BCAM Polyclonal Antibody(Capture/Detector) (AN003140P)
For research use only.
Verified Samples |
Verified Samples in ELISA: Recombinant Human BCAM protein, Human serum, Human plasma Verified Samples in WB: A431, LnCap |
Dilution | ELISA Capture 2-8 μg/mL, ELISA Detector 0.1-0.4 μg/mL, WB 1:500-1:1000 |
Isotype | Rabbit IgG |
Host | Rabbit |
Reactivity | Human |
Applications | ELISA Capture/Detector, WB |
Clonality | Polyclonal |
Immunogen | Recombinant Human BCAM Protein expressed by Mammalian |
Abbre | BCAM |
Synonyms | MSK, BCAM, AU, CD239, LU, MSK19, Auberger B antigen, Basal cell adhesion molecule, B-CAM cell surface glycoprotein, F8/G253 antigen, Lutheran antigen, Lutheran blood group glycoprotein, Rh30CE, Antigen identified by monoclonal F8, B CAM cell surface glycoprotein, B cell adhesion molecule, Basal cell adhesion molecule (Lu and Au blood groups), Basal cell adhesion molecule (Lutheran blood group), Basal cell adhesion molecule Lu and Au blood groups, Basal cell adhesion molecule Lutheran blood group, CD239 antigen, Glycoprotein 95kDa, Lutheran, Lutheran blood group (Auberger b antigen included), Lutheran blood group Auberger b antigen included |
Swissprot | |
Calculated MW | 67 kDa |
Observed MW |
85 kDa
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. |
Concentration | 1 mg/mL |
Buffer | Phosphate buffered solution, pH 7.2, containing 0.05% proclin 300. |
Purification Method | Antigen Affinity Purification |
Research Areas | Cardiovascular, Immunology |
Conjugation | Unconjugated |
Storage | Store at 4°C valid for 12 months or -20°C valid for long term storage, avoid freeze / thaw cycles. |
Shipping | The product is shipped with ice pack, upon receipt, store it immediately at the temperature recommended. |
background | This gene encodes Lutheran blood group glycoprotein, a member of the immunoglobulin superfamily and a receptor for the extracellular matrix protein, laminin. The protein contains five extracellular immunoglobulin domains, a single transmembrane domain, and a short C-terminal cytoplasmic tail. This protein may play a role in epithelial cell cancer and in vaso-occlusion of red blood cells in sickle cell disease. Polymorphisms in this gene define some of the antigens in the Lutheran system and also the Auberger system. Inactivating variants of this gene result in the recessive Lutheran null phenotype, Lu(a-b-), of the Lutheran blood group. Two transcript variants encoding different isoforms have been found for this gene. |
Other Clones
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Unconjugated
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