Jagged 1 Protein, Human, Recombinant (His Tag)

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Jagged 1 Protein, Human, Recombinant (His Tag): Product Information

Purity
> 85 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Measured by the ability of the immobilized protein to enhance BMP2-induced alkaline phosphatase activity in C3H10T1/2 mouse embryonic fibroblast cells.
The ED50 for this effect is typically 4-20 μg/mL.
Protein Construction
A DNA sequence encoding the human JAG1 (NP_000205.1) extracellular domain (Met 1-Ser 1046) was expressed, fused with a polyhistidine tag at the C-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Gln 34
Molecule Mass
The recombinant human JAG1 consists of 1024 amino acids and has a predicted molecular mass of 112 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh JAG1 is approximately 160-180 kDa due to glycosylation.
Formulation
Lyophilized from sterile PBS, pH 7.4
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Jagged 1 Protein, Human, Recombinant (His Tag): Images

Measured by the ability of the immobilized protein to enhance BMP2-induced alkaline phosphatase activity in C3H10T1/2 mouse embryonic fibroblast cells. The ED50 for this effect is typically 4-20 μg/mL.

Jagged 1 Protein, Human, Recombinant (His Tag): Alternative Names

AGS Protein, Human; AHD Protein, Human; AWS Protein, Human; CD339 Protein, Human; HJ1 Protein, Human; Jagged 1 Protein, Human; JAGL1 Protein, Human

Jagged 1 Background Information

Protein Jagged 1, also known as JAG1, JAGL1 and CD339, is a single-pass type I membrane protein which contains 1DSL domain and 15EGF-like domains. JAG1/Jagged 1 is widely expressed in adult and fetal tissues. The expression of JAG1/Jagged 1 is up-regulated in cervical squamous cell carcinoma. JAG1/Jagged 1 is also expressed in bone marrow cell line HS-27a which supports the long-term maintenance of immature progenitor cells. JAG1/Jagged 1 is a ligand for multiple Notch receptors. It is involved in the mediation of Notch signaling. JAG1/Jagged 1 may be involved in cell-fate decisions during hematopoiesis. JAG1/Jagged 1 seems to be involved in early and late stages of mammalian cardiovascular development. It inhibits myoblast differentiation and enhances fibroblast growth factor-induced angiogenesis. Defects in JAG1/Jagged 1 are the cause of Alagille syndrome type 1 (ALGS1). Alagille syndrome is an autosomal dominant multisystem disorder defined clinically by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. Defects in JAG1/Jagged 1 are also a cause of tetralogy of Fallot (TOF). TOF is a congenital heart anomaly which consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left) and hypertrophy of the right ventricle. This condition results in a blue baby at birth due to inadequate oxygenation.
Full Name
jagged 1
References
  • Oda T.et al., 1997, Nat. Genet. 16:235-242.
  • Krantz I.D. et al., 1998, Am. J. Hum. Genet. 62:1361-1369.
  • Li L. et al., 1998, Immunity. 8:43-55.
  • Jones E.A. et al., 2000, J. Med. Genet. 37: 658-662.
  • Roepke A.et al., 2003, Hum. Mutat. 21:100-100.
  • Jurkiewicz D.et al., 2005, Hum. Mutat. 25:321-321.
  • Warthen D.M.et al., 2006, Hum. Mutat. 27:436-443.
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