Recombinant CD38 Monoclonal Antibody (AN300945L)
For research use only.
| Verified Samples | Verified Samples in WB: Mouse spleen |
| Dilution | WB 1:1000-1:5000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human CD38 protein |
| Abbre | CD38 |
| Synonyms | cADPr hydrolase, ADP-ribosyl cyclase, cyclic ADP-ribose hydrolase, Acute lymphoblastic leukemia cells antigen CD, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase, CD38, ADPRC 1, ADPRC1, Acute lymphoblastic leukemia cells antigen CD38, ADP ribosyl cyclase, ADP-ribosyl cyclase 1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1, cADPr hydrolase 1, CD38 antigen, CD38 molecule, CD38H, Cyclic ADP ribose hydrolase, EC 3.2.2.5, I-19, NIMR5 antigen, p45, ADP-ribosyl, T10, cyclase, 2'-phospho-ADP-ribosyl cyclase, 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase, 2'-phospho-cyclic-ADP-ribose transferase, ADP-ribosyl cyclase 1 (ADPRC 1), Cyclic ADP-ribose hydrolase 1 (cADPr hydrolase 1), cyclic ADP-ribose hydrolase 1, ADP-ribosyl cyclase, ADP ribosyl cyclase, ADPRC1, CD38 antigen, CD38 molecule, CD38H, Cyclic ADP ribose hydrolase, EC 3.2.2.5, I-19, NIMR5 antigen, p45, T10, Acute lymphoblastic leukemia cells antigen CD38, ADP ribosyl cyclase, ADPRC1, CD38 antigen, CD38 molecule, CD38H, Cyclic ADP ribose hydrolase, EC 3.2.2.5, I-19, NIMR5 antigen, p45, T10, ADP ribosyl cyclase 1, ADP ribosyl cyclase/cyclic ADP-ribose hydrolase, CD 38, CD38 antigen (p45), Cd38-rs1, Cyclic ADP ribose hydrolase 1, Ecto nicotinamide adenine dinucleotide glycohydrolase, I19 (mouse), Lymphocyte differentiation antigen CD38, NAD(+) nucleosidase, NIM-R5 antigen, NIMR5 antigen (mouse), OTTHUMP00000158633, OTTHUMP00000217743 |
| Swissprot | |
| Calculated MW | 34 kDa |
| Observed MW |
45 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. |
| Cellular Localization | Membrane |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Immunology, Stem Cells, Cancer, Metabolism |
| Clone No. | 3F10 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | The protein encoded by this gene is a non-lineage-restricted, type II transmembrane glycoprotein that synthesizes and hydrolyzes cyclic adenosine 5'-diphosphate-ribose, an intracellular calcium ion mobilizing messenger. The release of soluble protein and the ability of membrane-bound protein to become internalized indicate both extracellular and intracellular functions for the protein. This protein has an N-terminal cytoplasmic tail, a single membrane-spanning domain, and a C-terminal extracellular region with four N-glycosylation sites. Crystal structure analysis demonstrates that the functional molecule is a dimer, with the central portion containing the catalytic site. It is used as a prognostic marker for patients with chronic lymphocytic leukemia. Alternative splicing results in multiple transcript variants. |
Other Clones
{{antibodyDetailsPage.numTotal}} Results
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
Other Formats
{{formatDetailsPage.numTotal}} Results
Unconjugated
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
-
IF：{{item.impact}}
Journal：{{item.journal}} ({{item.year}})
DOI：{{item.doi}}Reactivity：{{item.species}}
Sample Type：{{item.organization}}
-
Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}
