HLA Class I Rabbit Polyclonal Antibody

Description: Mouse monoclonal HLA MHC Class I antibody

Description: Rabbit polyclonal to HLA Class I.

Description: Rabbit polyclonal to HLA Class I.

Description: Antibody raised against HLA class I(HLA-A)

Description: Antibody raised against HLA class I(HLA-A)

Description: Antibody raised against HLA class I(HLA-B)

Description: Antibody raised against HLA class I(HLA-C)

Description: HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described.

Description: HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described.

Description: HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described.

Description: HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described.

Description: HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described.

Description: HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described.

Description: This mAb recognizes the HLA-B27 cell surface antigen on human cells. It may be used to HLA type human lymphocytes. Approximately 60% of patients with ankylosing spondylitis are HLA-B27 positive. This reagent can be used to help identify this HLA haplotype in human lymphocytes. Major histocompatibility complex (MHC) molecules form an integral part of the immune response system. They are cell-surface receptors that bind pep- tides and present them to T lymphocytes. Human leukocyte antigens (HLAs) are polymorphic members of the MHC family that are specifically involved in the presentation of antigens to the T cell receptor. There are two classes of HLA antigens: class I (HLA-A, HLA-B and HLA-C) and class II (HLA-D). Class I molecules are expressed in nearly all cells and play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum. The differential structural properties of MHC class I and class II molecules account for their respective roles in activating different populations of T lymphocytes. HLA-B encodes a membrane anchored heavy chain, which hetero-dimerizes with a light chain (b-2-Microglobulin) to form MHC-I. Polymorphisms yield hundreds of HLA-B alleles. The HLA-B27 allele appears with increased frequency in uveitis patients.

Description: This mAb recognizes the HLA-B27 cell surface antigen on human cells. It may be used to HLA type human lymphocytes. Approximately 60% of patients with ankylosing spondylitis are HLA-B27 positive. This reagent can be used to help identify this HLA haplotype in human lymphocytes. Major histocompatibility complex (MHC) molecules form an integral part of the immune response system. They are cell-surface receptors that bind pep- tides and present them to T lymphocytes. Human leukocyte antigens (HLAs) are polymorphic members of the MHC family that are specifically involved in the presentation of antigens to the T cell receptor. There are two classes of HLA antigens: class I (HLA-A, HLA-B and HLA-C) and class II (HLA-D). Class I molecules are expressed in nearly all cells and play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum. The differential structural properties of MHC class I and class II molecules account for their respective roles in activating different populations of T lymphocytes. HLA-B encodes a membrane anchored heavy chain, which hetero-dimerizes with a light chain (b-2-Microglobulin) to form MHC-I. Polymorphisms yield hundreds of HLA-B alleles. The HLA-B27 allele appears with increased frequency in uveitis patients.

Description: This mAb recognizes the HLA-B27 cell surface antigen on human cells. It may be used to HLA type human lymphocytes. Approximately 60% of patients with ankylosing spondylitis are HLA-B27 positive. This reagent can be used to help identify this HLA haplotype in human lymphocytes. Major histocompatibility complex (MHC) molecules form an integral part of the immune response system. They are cell-surface receptors that bind pep- tides and present them to T lymphocytes. Human leukocyte antigens (HLAs) are polymorphic members of the MHC family that are specifically involved in the presentation of antigens to the T cell receptor. There are two classes of HLA antigens: class I (HLA-A, HLA-B and HLA-C) and class II (HLA-D). Class I molecules are expressed in nearly all cells and play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum. The differential structural properties of MHC class I and class II molecules account for their respective roles in activating different populations of T lymphocytes. HLA-B encodes a membrane anchored heavy chain, which hetero-dimerizes with a light chain (b-2-Microglobulin) to form MHC-I. Polymorphisms yield hundreds of HLA-B alleles. The HLA-B27 allele appears with increased frequency in uveitis patients.