Biotinylated Recombinant Human Early Activation Antigen Cd69 (CD69) Protein (MBP&His-Avi)

Name: Biotinylated Recombinant Human Early Activation Antigen Cd69 (CD69) Protein (MBP&His-Avi)
Brand: Beta LifeScience
SKU: BLC-06529P
Price: 299.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Price Save $347

Size

100ug

Product Overview

Description	Biotinylated Recombinant Human Early Activation Antigen Cd69 (CD69) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q07108
Target Symbol	CD69
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-MBP&C-6His-Avi
Target Protein Sequence	SVGQYNCPGQYTFSMPSDSHVSSCSEDWVGYQRKCYFISTVKRSWTSAQNACSEHGATLAVIDSEKDMNFLKRYAGREEHWVGLKKEPGHPWKWSNGKEFNNWFNVTGSDKCVFLKNTEVSSMECEKNLYWICNKPYK
Expression Range	62-199aa
Protein Length	Partial
Mol. Weight	63.7 kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets.
Subcellular Location	Membrane; Single-pass type II membrane protein.
Database References	HGNC: 1694 OMIM: 107273 KEGG: hsa:969 STRING: 9606.ENSP00000228434 UniGene: Hs.208854
Tissue Specificity	Expressed on the surface of activated T-cells, B-cells, natural killer cells, neutrophils, eosinophils, epidermal Langerhans cells and platelets.

Gene Functions References

CD69 is a direct target of miR-367-3p. PMID: 30015935
The frequency of CD69+ T cells was significantly higher in CD8+ and CD4+ T cells in nasal polyps compared with the peripheral blood of patients with chronic rhinosinusitis. PMID: 29749428
this paper shows that decrease of CD69 levels on TCR Valpha7.2(+)CD4(+) innate-like lymphocytes is associated with impaired cytotoxic functions in chronic hepatitis B virus-infected patients PMID: 28606013
AIM expression in the kidney was associated with urinary protein and decline in kidney function. PMID: 26846784
Higher CD69 expression were less sensitive to bendamustine and is associated with chronic lymphocytic leukemia. PMID: 26701728
In vitro functional assays showed that CD69(+) Treg cells exerted an important suppressive effect on the activation of T effector cells PMID: 26100786
results demonstrate the functional and mechanistic interplays between CD69 and S100A8/S100A9 in supporting Treg-cell differentiation PMID: 26296369
Elevated expression of CD69 and CD161 on NK cells can be considered as immunological risk markers in RSA and IVF failure. PMID: 24975965
these findings identify CD69 and galectin-1 to be a novel regulatory receptor-ligand pair that modulates Th17 effector cell differentiation and function. PMID: 24752896
REVIEW: CD69 exerts a complex immunoregulatory role in humans, and that it could be considered as a target molecule for the therapy of immune-mediated diseases PMID: 23954168
Following coculture with GTKO/CD46 pig mesenchymal stromal cells, it is possible that upregulation of CD69 on human T cells initiates signaling events that would regulate CD4+ and CD8+ T cell activation and differentiation. PMID: 24044963
In patients with allergic rhinitis CD69 antigen is overexpressed on human peripheral blood natural killer cells reflecting their activation status. PMID: 23454781
This is the first report of the regulation of CD69 expression by LMP-1, and this novel finding may, thus, represent an important link between the EBV oncoprotein LMP-1 and its critical role in the development of EBV-associated diseases. PMID: 23546309
CD69 is induced by integrin alpha4beta1 outside-in signalling and T-cell receptor signalling. PMID: 23758320
CD69 overexpression is associated with the human T-cell leukemia virus type 1 infection and adult T-cell leukemia. PMID: 23507197
Intron I acts as an important regulatory element of CD69 expression. PMID: 22456278
CD69 is significantly correlated with poor clinical and biological prognostic factors and is confirmed to be an independent disease prognosticator in chronic lymphocytic leukemia. PMID: 21993667
Priming with apoptotic debris prevented DCs from establishing cytotoxicity toward live human tumor cells by inducing a Treg-cell population, defined by coexpression of CD39 and CD69 PMID: 22678911
T cells isolated from the hepatocellular carcinoma tissues expressed significantly more CD69 molecules than did those on paired circulating and nontumor-infiltrating T cells; these tumor-derived CD69(+) T cells could induce considerable IDO in monocytes PMID: 22184722
Results suggest that H. pylori induces CD69 expression through the activation of NF-kappaB, and that cagPAI might be relevant in the induction of CD69 expression in T cells. CD69 in T cells may play a role in H. pylori-induced gastritis. PMID: 21990950
Caffeine does not appear to depress Natural killer cell CD69 expression. PMID: 21152932
Studies provide a mechanistic link between CD69 and the regulation of T(H)17 responses. PMID: 21427408
The expression of CD69 in T lymphocytes from nasal polyps was abnormally high. PMID: 15952571
structure refined to 1.37 A resolution provides further details of the overall structure and the asymmetric interface between the monomers in the native dimer PMID: 20054122
analysis of CD69 molecules on human CD4+ T cell membrane PMID: 19670272
CD69 engagement initiates protein tyrosine kinase-dependent signaling pathways in IL-2-activated NK cells by inducing selective activation of Syk, but not ZAP70, kinase. PMID: 12077230
CD69 transduces a Bcl-2-dependent death signal when ligated by a specific antibody. As the function of CD69 appears to be restricted to activated eosinophils, making an ideal target for therapeutic intervention in asthma. PMID: 12234263
a higher CD69 expression when atopic neutrophils were incubated with GM-CSF compared to non-atopic neutrophils PMID: 12540017
GM-CSF, IFN-gamma or IFN-alpha significantly induced CD69 expression on neutrophils. We demonstrated the capacity of CD69 to act as a costimulus for TNF-alpha production by neutrophils. PMID: 12718936
expression of CD69 on CD3+ and CD8+ peripheral blood T cells correlates closely with the presence of acute graft rejection in renal allograft recipients PMID: 12865808
Increased CD69 of T lymphocytes, along with abnormally elevated immunologically active molecules play an important role in immune pathogenesis of patients with myelodysplastic syndrome(MDS). PMID: 14728878
CD69 forms a complex with and negatively regulates S1P1 and that it functions downstream of IFN-alpha/beta, and possibly other activating stimuli, to promote lymphocyte retention in lymphoid organs PMID: 16525420
Plasmodium falciparum histidine-rich protein II reduces CD69 expression in T cells. PMID: 16788832
data suggest unidentified natural ligands for CD69 and/or CD69 autoantibodies possibly affect joint-composing cell types through increased production of S100A9 in neutrophils, providing insight into functions of CD69 on neutrophils in rheumatoid arthritis PMID: 17237603
IL-3 is a central inducer of CD69 expression. Upregulated CD69 expression on locally accumulated basophils in bronchial asthma may be partly due to a combination of local cytokines, especially IL-3, plus IgE-cross-linking allergens. PMID: 17541278
Since induction of CD69 surface expression is dependent on the activation of the protein kinase C (PKC) activation pathway, it is suggested that in chronic fatigue syndrome there is a disorder in the early activation of the immune system involving PKC. PMID: 17693977
results do not support a major role for the CD69 gene polymorphisms in RA genetic predisposition in our population. PMID: 18627570
the physical, biochemical and in vivo characteristics of a highly stable soluble form of CD69 obtained by bacterial expression of an appropriate extracellular segment of this protein. PMID: 18959746
Expression of CD69 and IL8 is upregulated upon Bcr-Abl expression PMID: 19383348
soluble factors in SSc plasma inhibit Treg function specifically that is associated with altered Treg CD69 and TGFbeta expression PMID: 19543397

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.