Name :
Human CD38-VLP (Full Length) Protein

Biological Activity :

Background :
The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Cluster of differentiation 38 (CD38), also known as ADP-ribosyl cyclase, is a glycoprotein found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B and natural killer cells. It shares several characteristics with ADP-ribosyl cyclase 2 CD157. CD38 is a multifunctional ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose (cADPR) from NAD+ to ADP-ribose. It also functions in cell adhesion, signal transduction and calcium signaling. CD38 has been used as a prognostic marker in leukemia. It can also be used to identify plasma cells.

Biological Activity :
Immobilized Recombinant Human CD38-VLP (Full Length) Protein (Cat: 10818-HNAH) at 2 μg/mL (100 μL/well) can bind Anti-CD38 Antibody, the EC50 is 3-9 ng/mL.

Expression Host :
Human

Source :
HEK293 Cells

Tag :

Protein Accession No. :
P28907

NCBI Gene ID :

Synonyms :

Synonyms :
CD38 molecule

Amino Acid Sequence :

Molecular Weight :
The recombinant Human CD38-VLP (Full Length) consists of 300 amino acids and predicts a molecular mass of 34.33 kDa.

Purity :

State of Matter :

Product Concentration :

Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -70℃. Store it under sterile conditions at -70℃ or lower. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Endotoxin Level :
< 1.0 EU per μg protein as determined by the LAL method.

Protein Construction :
A DNA sequence encoding the Human CD38-VLP (Full Length) (P28907) (Met1-Ile300) was expressed.

Buffer Solution :
Supplied as sterile 50mM Hepes, 150mM NaCl, 10% Trehalose, pH 7.2.Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.

Shipping :
It is supplied and shipped as liquid with dry ice.

Redissolution :

Synonyms :
ADPRC 1 Protein, Human; ADPRC1 Protein, Human; T10 Protein, Human CD38 背景信息 The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Cluster of differentiation 38 (CD38), also known as ADP-ribosyl cyclase, is a glycoprotein found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B and natural killer cells. It shares several characteristics with ADP-ribosyl cyclase 2 CD157. CD38 is a multifunctional ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose (cADPR) from NAD+ to ADP-ribose. It also functions in cell adhesion, signal transduction and calcium signaling. CD38 has been used as a prognostic marker in leukemia. It can also be used to identify plasma cells.

References & Citations :
Zola H, et al. (2007) CD molecules 2006-human cell differentiation molecules. J Immunol Methods. 318 (1-2): 1-5.Ho IC, et al. (2009) GATA3 and the T-cell lineage: essential functions before and after T-helper-2-cell differentiation. Nat Rev Immunol. 9 (2): 125-35.Matesanz-Isabel J, et al. (2011) New B-cell CD molecules. Immunology Letters.134 (2): 104-12.

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