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For research use only.

Verified Samples Verified Samples in WB: Raji, Human spleen
Verified Samples in IHC: Human prostate cancer
Dilution WB 1:500-1:2000,  IHC 1:50-1:300
Isotype IgG
Host Rabbit
Reactivity Human
Applications WB,  IHC
Clonality Polyclonal
Immunogen Fusion protein of human HLA-DRB1
Abbre HLA-DRB1
Synonyms Human Leucocyte Antigen DRB1,  MHC Class II Antige,  MHC Class II Antigen DRB1*10,  MHC Class II Antigen DRB1*11,  MHC Class II Antigen DRB1*12,  MHC Class II Antigen DRB1*13,  MHC Class II Antigen DRB1*14,  MHC Class II Antigen DRB1*15,  MHC Class II HLA-DR Beta 1 Chain
Swissprot
Calculated MW 30 kDa
Observed MW Refer to figures
The actual band is not consistent with the expectation.

Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include:

1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein.

2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes.

3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1.

4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids).

5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers.

If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane.

Cellular Localization Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, MHC II.
Concentration 1.32 mg/mL
Buffer Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol.
Purification Method Antigen affinity purification
Research Areas Immunology
Conjugation Unconjugated
Storage Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
Shipping The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended.
background HLA-DRB1 belongs to the HLA class II beta chain paralogs. The class II molecule is a heterodimer consisting of an alpha (DRA) and a beta chain (DRB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa. It is encoded by 6 exons. Exon one encodes the leader peptide; exons 2 and 3 encode the two extracellular domains; exon 4 encodes the transmembrane domain; and exon 5 encodes the cytoplasmic tail. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Hundreds of DRB1 alleles have been described and typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. DRB1 is expressed at a level five times higher than its paralogs DRB3, DRB4 and DRB5. DRB1 is present in all individuals. Allelic variants of DRB1 are linked with either none or one of the genes DRB3, DRB4 and DRB5. There are 4 related pseudogenes: DRB2, DRB6, DRB7, DRB8 and DRB9.
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Unconjugated

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