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1000 results found for “GHRP”
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Name :
EGF HumanDescription:
Epidermal Growth Factor Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-217Price :
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Shipped at Room temp
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Description
Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.
Citations
More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
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Background
About EGF:
In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF).
Description:
Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses.
Function:
By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers.
Mechanism:
EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.
What is the source or expression system of EGF Protein?
Escherichia Coli.
What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.
What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SSTDescription:
Somatostatin
Growth hormone release-inhibiting factor, SST, SMS, SMST, GHIH.
Product # :
HOR-299Price :
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Shipped at Room temp
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Description
Somatostatin Synthetic is a single, non-glycosylated polypeptide chain containing 14 amino acids, having a molecular mass of 1637.9 Dalton and a Molecular formula of C76H104N18O19S2. The CAS# is 38916-34-6.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Somatostatin (also known as growth hormone inhibiting hormone (GHIH) or somatotropin release-inhibiting hormone (SRIF) is a peptide hormone that regulates the endocrine systemand affects neurotransmission and cell proliferation via interaction with G-protein-coupled somatostatin receptors and inhibition of the release of numerous secondary hormones. Somatostatin has two active forms produced by alternative cleavage of a single preproprotein: one of 14 amino acids, the other of 28 amino acids.
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Synonyms
Growth hormone release-inhibiting factor, SST, SMS, SMST, GHIH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SST although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Somatostatin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Somatostatin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Ala-Gly-Cys-Lys-Asn-Phe- Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys-OH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IGFBP 1 HumanDescription:
Insulin-Like Growth Factor Binding Protein-1 Human Recombinant
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.
Product # :
CYT-299Price :
Quantity :
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Shipped at Room temp
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Description
IGFBP-1 Human Recombinant (26-259 a.a.) produced in NS0 is a single, glycosylated, polypeptide chain containing 234 amino acids and having a molecular mass of 25kDa. The IGFBP1 is purified by proprietary chromatographic techniques.
Source
Mouse myeloma cell line, NS0.
Formulation
IGFBP-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.Citations
More Info
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Introduction
IGFBP1 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
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Synonyms
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGFBP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF-BP1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized IBP-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.
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Background
What is the molecular weight/Mw of IGFBP1 HUMAN Protein?
IGFBP1 HUMAN Protein has a total Mw of 25kDa.
What is the source or expression system of IGFBP1 HUMAN Protein?
Mouse myeloma cell line, NS0.
What is the Purity of IGFBP1 HUMAN Protein?
IGFBP1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IGFBP1 HUMAN Protein?
The ED50, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.
What is the amino acid sequence of IGFBP1 HUMAN Protein?
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.
What applications can IGFBP1 HUMAN Protein be used in?
IGFBP1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGFBP1 HUMAN Protein?
The endotoxin level is minimal, IGFBP1 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SHH RatDescription:
Sonic HedgeHog Rat Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Product # :
CYT-1099Price :
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Shipped at Room temp
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Description
Sonic HedgeHog Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.9kDa. SHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SHH is lyophilized from a sterile (0.2 µm) filtered solution containing 10 mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog helps in guiding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is necessary for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
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Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SHH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MIIGPGRGFG KRQHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKARI HCSVKAENSV AAKSDG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CSRP2 HumanDescription:
Cysteine and Glycine-rich Protein 2 Human Recombinant
Cysteine and glycine-rich protein 2, Smooth muscle cell LIM protein, LIM domain only 5 smooth muscle, SmLIM, LMO5, CRP2.
Product # :
PRO-1096Price :
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Shipped with Ice Packs
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Description
CSRP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 217 amino acids (1-193) and having a molecular mass of 23.5kDa.CSRP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CSRP2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CSRP2 belongs to the CSRP family. CSRP2 holds 2 LIM zinc-binding domains that take part in regulatory processes essential for development and cellular differentiation. Additionally, CSRP2 is involved in the development of the embryonic vascular system.
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Synonyms
Cysteine and glycine-rich protein 2, Smooth muscle cell LIM protein, LIM domain only 5 smooth muscle, SmLIM, LMO5, CRP2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPVWGG GNKCGACGRT VYHAEEVQCD GRSFHRCCFL CMVCRKNLDS TTVAIHDEEI YCKSCYGKKY GPKGYGYGQG AGTLNMDRGE RLGIKPESVQ PHRPTTNPNT SKFAQKYGGA EKCSRCGDSV YAAEKIIGAG KPWHKNCFRC AKCGKSLEST TLTEKEGEIY CKGCYAKNFG PKGFGYGQGA GALVHAQ
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NRGN HumanDescription:
Neurogranin Human Recombinant
hng, RC3, Neurogranin, Ng, NRGN.
Product # :
CYT-293Price :
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Shipped with Ice Packs
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Description
NRGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a.) and having a molecular mass of 10.0kDa (molecular size on SDS-PAGE will appear higher). NRGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NRGN protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH7.0), 30% glycerol 0.1mM PMSF and 1mM EDTA.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Neurogranin (NRGN) is a calmodulin-binding protein which is expressed solely in the brain, mainly in dendritic spines. NRGN is also taking part in the protein kinase C signaling pathway by being a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. NRGN binds to calmodulin in the absence of calcium. NRGN protein’s phosphorylation by protein kinase C lowers its binding ability.
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Synonyms
hng, RC3, Neurogranin, Ng, NRGN.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDCCTEN ACSKPDDDIL DIPLDDPGAN AAAAKIQASF RGHMARKKIK SGERGRKGPG PGGPGGAGVA RGGAGGGPSG D.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FABP5 Human, HisDescription:
Fatty Acid Binding Protein 5 Human Recombinant, His Tag
Fatty acid-binding protein epidermal, E-FABP, Fatty acid-binding protein 5, Psoriasis-associated fatty acid-binding protein homolog, PA-FABP, FABP5, EFABP, PAFABP.
Product # :
PRO-666Price :
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Shipped with Ice Packs
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Description
FABP5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 19.66kDa. FABP5 is fused to His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
FABP5 His-Tag is supplied in 20mM Tris HCl pH-8 and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Human Fatty Epidermal Acid Binding Protein FABP also called FABP-5 is a 15 kD member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds ( bile acids or retinoids). In an internal cavity. The fatty acid binding proteins aP2 (fatty acid binding protein [FABP]-4) and mal1 (EFABP) are closely related and both are expressed in adipocytes. Absence of EFABP/mal1 resulted in increased systemic insulin sensitivity in two models of obesity and insulin resistance. Adipocytes isolated from mal1-deficient mice also exhibited enhanced insulin-stimulated glucose transport capacity. In contrast, mice expressing high levels of mal1 in adipose tissue display reduced systematic insulin activity.
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Synonyms
Fatty acid-binding protein epidermal, E-FABP, Fatty acid-binding protein 5, Psoriasis-associated fatty acid-binding protein homolog, PA-FABP, FABP5, EFABP, PAFABP.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PGLYRP1 HumanDescription:
Peptidoglycan Recognition Protein 1 Human Recombinant
Peptidoglycan recognition protein 1, Peptidoglycan recognition protein short, PGRP-S, PGLYRP1, PGLYRP, PGRP, TNFSF3L, TAG7, PGRPS.
Product # :
PRO-1597Price :
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Shipped at Room temp
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Description
PGLYRP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-196) containing 185 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 20.68kDa (calculated).
Source
Escherichia Coli.
Formulation
PGLYRP1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Peptidoglycan Recognition Protein 1 (PGLYRP1) is a member of the N-acetylmuramoyl-L-alanine amidase 2 family. PGLYRP1 binds to peptidoglycan of bacteria and affects the peptidoglycan biosynthesis. PGLYRP1 displays bactericidal activity towards Gram-positive bacteria and is bacteriostatic towards Gram-negative bacteria. PGLYRP1 has a role in innate immunity. PGLYRP1 is highly expressed in the bone marrow, and weakly expressed in the kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils.
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Synonyms
Peptidoglycan recognition protein 1, Peptidoglycan recognition protein short, PGRP-S, PGLYRP1, PGLYRP, PGRP, TNFSF3L, TAG7, PGRPS.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely at 37°C. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. PGLYRP1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASQETEDPACCS PIVPRNEWKA LASECAQHLS LPLRYVVVSH TAGSSCNTPA SCQQQARNVQ HYHMKTLGWC DVGYNFLIGE DGLVYEGRGW NFTGAHSGHL WNPMSIGISF MGNYMDRVPT PQAIRAAQGL LACGVAQGAL RSNYVLKGHR DVQRTLSPGN QLYHLIQNWP HYRSP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TGFBR2 Human, HisDescription:
Transforming Growth Factor Beta Receptor II, His Tag Human Recombinant
AAT3, FAA3, MFS2, RIIC, LDS1B, LDS2B, TAAD2, TGFR-2, TGFbeta-RII, TGFBR-2, TGF-beta receptor type-2, Transforming growth factor-beta receptor type II, TGF-beta receptor type II, TGF-beta type II receptor, TbetaR-II, TGFBR2.
Product # :
PKA-088Price :
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Description
TGFBR2 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 383 amino acids (23-166a.a) and having a molecular mass of 43.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TGFBR2 is expressed with a 239aa hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The TGFBR2 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TGFBR2 is part of the Ser/Thr protein kinase family and the TGFB receptor subfamily. TGFBR2 is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 expression is increased in oral squamous cell carcinoma cells. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity of tamoxifen metabolites in breast cancer.
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Synonyms
AAT3, FAA3, MFS2, RIIC, LDS1B, LDS2B, TAAD2, TGFR-2, TGFbeta-RII, TGFBR-2, TGF-beta receptor type-2, Transforming growth factor-beta receptor type II, TGF-beta receptor type II, TGF-beta type II receptor, TbetaR-II, TGFBR2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
TIPPHVQKSV NNDMIVTDNN GAVKFPQLCK FCDVRFSTCD NQKSCMSNCS ITSICEKPQE VCVAVWRKND ENITLETVCH DPKLPYHDFI LEDAASPKCI MKEKKKPGET FFMCSCSSDE CNDNIIFSEE YNTSNPDLLL VIFQLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TIRAP HumanDescription:
Toll-Interleukin 1 Receptor (TIR) Domain Containing Adaptor Protein Human Recombinant
Toll-interleukin 1 receptor (TIR) domain containing adaptor protein, adapter protein wyatt, BACTS1, Mal, wyatt, Toll-like receptor adaptor protein, TIR domain-containing adapter protein, MyD88 adapter-like protein.
Product # :
PRO-1181Price :
Quantity :
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Shipped with Ice Packs
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Description
TIRAP Human Recombinant produced in E. coli is a single polypeptide chain containing 244 amino acids (1-221) and having a molecular mass of 26.3 kDa.TIRAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TIRAP solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Toll-interleukin1 receptor (TIR) domain containing adaptor protein (TIRAP) contains 1 TIR domain. TIRAP is an adapter molecule linked with toll-like receptors. TIRAP is required in TLR2 and TLR4 signaling pathways in the innate immune response. TIRAP activates NF-kappa-B, MAPK1, MAPK3 and JNK, which subsequently results in cytokine secretion and the inflammatory response. TIRAP is highly expressed in the liver, kidney, spleen, skeletal muscle and heart. TIRAP is also found in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.
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Synonyms
Toll-interleukin 1 receptor (TIR) domain containing adaptor protein, adapter protein wyatt, BACTS1, Mal, wyatt, Toll-like receptor adaptor protein, TIR domain-containing adapter protein, MyD88 adapter-like protein.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASSTSL PAPGSRPKKP LGKMADWFRQ TLLKKPKKRP NSPESTSSDA SQPTSQDSPL PPSLSSVTSP SLPPTHASDS GSSRWSKDYD VCVCHSEEDL VAAQDLVSYL EGSTASLRCF LQLRDATPGG AIVSELCQAL SSSHCRVLLI TPGFLQDPWC KYQMLQALTE APGAEGCTIP LLSGLSRAAY PPELRFMYYV DGRGPDGGFR QVKEAVMRYL QTLS
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
POR HumanDescription:
P450 Oxidoreductase Human Recombinant
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
Product # :
ENZ-890Price :
Quantity :
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Shipped with Ice Packs
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Description
POR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 686 amino acids (1-680a.a.) and having a molecular mass of 77.9kDa. POR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
POR protein solution (0.25mg/ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.
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Synonyms
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MINMGDSHVD TSSTVSEAVA EEVSLFSMTD MILFSLIVGL LTYWFLFRKK KEEVPEFTKI QTLTSSVRES SFVEKMKKTG RNIIVFYGSQ TGTAEEFANR LSKDAHRYGM RGMSADPEEY DLADLSSLPE IDNALVVFCM ATYGEGDPTD NAQDFYDWLQ ETDVDLSGVK FAVFGLGNKT YEHFNAMGKY VDKRLEQLGA QRIFELGLGD DDGNLEEDFI TWREQFWLAV CEHFGVEATG EESSIRQYEL VVHTDIDAAK VYMGEMGRLK SYENQKPPFD AKNPFLAAVT TNRKLNQGTE RHLMHLELDI SDSKIRYESG DHVAVYPAND SALVNQLGKI LGADLDVVMS LNNLDEESNK KHPFPCPTSY RTALTYYLDI TNPPRTNVLY ELAQYASEPS EQELLRKMAS SSGEGKELYL SWVVEARRHI LAILQDCPSL RPPIDHLCEL LPRLQARYYS IASSSKVHPN SVHICAVVVE YETKAGRINK GVATNWLRAK EPVGENGGRA LVPMFVRKSQ FRLPFKATTP VIMVGPGTGV APFIGFIQER AWLRQQGKEV GETLLYYGCR RSDEDYLYRE ELAQFHRDGA LTQLNVAFSR EQSHKVYVQH LLKQDREHLW KLIEGGAHIY VCGDARNMAR DVQNTFYDIV AELGAMEHAQ AVDYIKKLMT KGRYSLDVWS HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Guanylin HumanDescription:
Guanylin Human Recombinant
Guanylin, GUCA2A, Gap-IGUCA2, STARA, GUANYLIN.
Product # :
HOR-281Price :
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Shipped at Room temp
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Description
Proguanylin Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain (a.a 22-115) containing 104 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 11.5kDa (calculated).
Source
Escherichia Coli.
Formulation
Proguanylin filtered (0.4 µm) and lyophilized in 0.5mg/ml in deionized H20.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Heat-stable enterotoxins (STa) are small, cysteine-rich peptides secreted by Escherichia coli that are able to induce diarrhea through the stimulation of an intestine-specific receptor-guanylyl cyclase known as STaR. Binding of STa to STaR induces a dramatic increase in the cGMP content of the cell; the increase, in turn, inhibits salt absorption and stimulates chloride secretion. This imbalance of ions is accompanied by a massive accumulation of water in the gut that gives rise to the diarrhea and dehydration characteristic of enterotoxin activity. The identification of a receptor for STa on intestinal brush border membranes suggested the existence of an endogenous activator, described guanylin, a 15-amino acid peptide purified from rat small intestine, as a potential ligand for the STaR. This peptide shares sequence similarity with STa; see also uroguanylin. The molecular cloning of the human and mouse cDNAs encoding guanylin was reported. The sequences demonstrated that guanylin is present at the C-terminal end of a larger precursor protein. Expression in mammalian cells indicated that the 94- amino acid proguanylin is inactive. The biologically active guanylin can be released by either chemical or enzymatic treatment of proguanylin. By Northern blot analysis and in situ hybridization, showed that expression of guanylin mRNA is restricted to cells of the intestinal epithelium, specifically the Paneth cells at the base of the small intestinal crypts. These results demonstrate that guanylin is an endogenous activator of STaR isolated a cDNA encoding an apparent precursor of guanylin from a human intestinal cDNA library. The mRNA was expressed at high levels in human ileum and colon. In the mouse, interspecific backcross analysis used to map the Guca2 gene to the distal half of mouse chromosome 4 in a region of homology with human chromosome 1p. By fluorescence in situ hybridization mapped the GUCA2 gene to human 1p35-p34 Guanylin is thought to modulate intestinal water/electrolyte transport in a paracrine mode reported the nucleotide sequence of the gene, the characteristics of its circulating molecular form, and its localization in enterochromaffin cells of the gut. The gene, approximately 2.6 kb in size, consists of 3 exons interrupted by 2 introns. The hormonal form of guanylin is a 94-amino acid peptide with a molecular mass of 10.3 kDa. Guanylin is synthesized by gut enterochromaffin cells as a prohormone of 115 amino acids and is processed to the molecular form of 94 amino acids circulating in the blood.
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Synonyms
Guanylin Precursor, Guanylate cyclase activator 2A, Guanylate cyclase-activating protein 1, Gap-IGUCA2, STARA, GUANYLIN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Proguanylin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS VTVQDGNFSF SLESVKKLKD LQEPQEPRVG KLRNFAPIPG EPVVPILCSN PNFPEELKPL CKEPNAQEIL QRLEEIAEDP GTCEICAYAA CTGC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CGREF1 HumanDescription:
Cell Growth Regulator With EF-Hand Domain 1 Human Recombinant
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.
Product # :
PRO-2154Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CGREF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (20-301 a.a) and having a molecular mass of 32.3kDa. CGREF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CGREF1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4).
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Cell Growth Regulator with EF-Hand Domain 1, also known as CGREF1 is a secreted calcium ion binding protein. CGREF1 includes two EF-hand domains & both EF-hands are essential for function. CGREF1 is most likely digested extracellularly by an unfamiliar serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is capable to inhibit growth in more than a few cell lines.
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Synonyms
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAPKDGVT RPDSEVQHQL LPNPFQPGQE QLGLLQSYLK GLGRTEVQLE HLSREQVLLY LFALHDYDQS GQLDGLELLS MLTAALAPGA ANSPTTNPVI LIVDKVLETQ DLNGDGLMTP AELINFPGVA LRHVEPGEPL APSPQEPQAV GRQSLLAKSP LRQETQEAPG PREEAKGQVE ARRESLDPVQ EPGGQAEADG DVPGPRGEAE GQAEAKGDAP GPRGEAGGQA EAEGDAPGPR GEAGGQAEAR ENGEEAKELP GETLESKNTQ NDFEVHIVQV ENDEI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PSAP HumanDescription:
Prosaposin Human Recombinant
Prosaposin, Proactivator polypeptide, PSAP, GLBA, SAP1.
Product # :
PRO-1600Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PSAP Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 17-524) containing a total of 518 amino acids, having a molecular mass of 57.7kDa (calculated), though it migrates at approximately 65kDa on SDS PAGE, the PSAP is fused to a 2 a.a N-terminal linker, a 2 a.a C-terminal linker and a 6 a.a His tag at C-Terminus.The Human PSAP is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in phosphate buffer, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Prosaposin (PSAP) is a precursor of 4 lysosomal saposin proteins (saposin A, B, C and D). Saposins are heat-stable glycoproteins which facilitate the catabolism of glycosphingolipids with short oligosaccharide groups. PSAP stimulates neurite outgrowth and increases choline acetyltransferase activity. Prosaposin exists both as a secretory protein and as an integral membrane protein and has neurotrophic activities. The secreted prosaposin is assumed to have additional functions in human milk, cerebrospinal fluid and seminal plasma. PSAP gene mutations are linked with Gaucher disease, Tay-Sachs disease, and metachromatic leukodystrophy.
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Synonyms
Prosaposin, Proactivator polypeptide, PSAP, GLBA, SAP1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. PSAP is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
ASGPVLGLKE CTRGSAVWCQ NVKTASDCGA VKHCLQTVWN KPTVKSLPCD ICKDVVTAAG DMLKDNATEE EILVYLEKTC DWLPKPNMSA SCKEIVDSYL PVILDIIKGE MSRPGEVCSA LNLCESLQKH LAELNHQKQL ESNKIPELDM TEVVAPFMAN IPLLLYPQDG PRSKPQPKDN GDVCQDCIQM VTDIQTAVRT NSTFVQALVE HVKEECDRLG PGMADICKNY ISQYSEIAIQ MMMHMQPKEI CALVGFCDEV KEMPMQTLVP AKVASKNVIP ALELVEPIKK HEVPAKSDVY CEVCEFLVKE VTKLIDNNKT EKEILDAFDK MCSKLPKSLS EECQEVVDTY GSSILSILLE EVSPELVCSM LHLCSGTRLP ALTVHVTQPK DGGFCEVCKK LVGYLDRNLE KNSTKQEILA ALEKGCSFLP DPYQKQCDQF VAEYEPVLIE ILVEVMDPSF VCLKIGACPS AHKPLLGTEK CIWGPSYWCQ NTETAAQCNA VEHCKRHVWN KLHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GPBB HumanDescription:
Glycogen Phosphorylase Human Recombinant
Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.
Product # :
ENZ-282Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Glycogen Phosphorylase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain. The Human GPBB mature chain: 2 - 843 aa; that is a total of 842 aa having a molecular mass of 96695.96 Dalton. The theoretical pI is 6.40.The GPBB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of protein contains 50% glycerol.
Purity
Greater than 85.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
Glycogen phosphorylase is one of the phosphorylaseenzymes(EC2.4.1.1). It breaks up glycogeninto glucosesubunits. Glycogenis left with one less glucosemolecule, and the free glucosemolecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphateby the enzyme phosphoglucomutase.
Glycogen phosphorylase can only act on linearchainsof glycogen(a 1-4 glycosidic linkage). Its work will immediately come to a halt four residues away from a 1-6 branch(which are exceedingly common in glycogen). In these situations, a debranching enzymeis necessary, which will straighten out the chain in that area. Additionally, an alpha 1-6 glucosidaseenzymeis required to break the remaining 1-6 residue that remains in the new linear chain. After all this is done, glycogen phosphorylase can continue.
An insulinstimulated enzyme known as phosphoprotein phosphatase(PP-1) inactivates glycogen phosphorylase to prevent glycogen break up.
GPBB - a sensitive marker for the AMI diagnosis within 4 hours after the onset of chest pain. It has also been shown that GPBB is increased in a considerable proportion of AMI patients within 2-3 hours from chest pain onset. GPBB is increased early in patients with unstable angina. GPBB can also be a sensitive marker for the detection of peri-operative myocardial ischaemia and infarction in patients undergoing coronary artery bypass grafting. -
Synonyms
Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.
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Physical Appearance
Sterile Filtered colourless liquid formualtion.
-
Stability
GPBB although stable at 10°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.
-
Applications
Immunoassays and western blot.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
M6PR HumanDescription:
Mannose-6-Phosphate Receptor Human Recombinant
Mannose-6-Phosphate Receptor (Cation Dependent), CD-MPR, MPR46, CD Man-6-P Receptor, MPR 46, 46-KDa Mannose 6-Phosphate Receptor, MPR-46, SMPR, Cation-Dependent Mannose-6-Phosphate Receptor, Mr 46,000 Man6PR, Small Mannose 6-Phosphate Receptor, 46 KDa Mannose 6-Phosphate Receptor, MPRD, M6PR.
Product # :
PRO-1961Price :
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Description
M6PR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (27-185) and having a molecular mass of 20.3kDa.M6PR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The M6PR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Mannose-6-Phosphate Receptor (M6PR) belongs to the P-type lectin family. P-type lectins play a vital role in lysosome function through the specific transport of mannose-6-phosphate-containing acid hydrolases from the Golgi complex to lysosomes. The M6PR protein functions as a homodimer and needs divalent cations for ligand binding. Lysosomal enzymes carrying phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the ensuing receptor-ligand complex is transferred to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex.
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Synonyms
Mannose-6-Phosphate Receptor (Cation Dependent), CD-MPR, MPR46, CD Man-6-P Receptor, MPR 46, 46-KDa Mannose 6-Phosphate Receptor, MPR-46, SMPR, Cation-Dependent Mannose-6-Phosphate Receptor, Mr 46,000 Man6PR, Small Mannose 6-Phosphate Receptor, 46 KDa Mannose 6-Phosphate Receptor, MPRD, M6PR.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTEEKTCD LVGEKGKESE KELALVKRLK PLFNKSFEST VGQGSDTYIY IFRVCREAGN HTSGAGLVQI NKSNGKETVV GRLNETHIFN GSNWIMLIYK GGDEYDNHCG KEQRRAVVMI SCNRHTLADN FNPVSEERGK VQDCFYLFEM DSSLACSPEI SH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CRIPT HumanDescription:
Cysteine-Rich PDZ-Binding Protein Human Recombinant
Cysteine-rich interactor of PDZ three, cysteine-rich PDZ-binding protein, Cysteine-rich interactor of PDZ3, postsynaptic protein CRIPT, HSPC139.
Product # :
PRO-1105Price :
Quantity :
Shipping Method :
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Description
CRIPT Human Recombinant produced in E. coli is a single polypeptide chain containing 124 amino acids (1-101) and having a molecular mass of 13.7kDa.CRIPT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CRIPT solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Cysteine-rich PDZ-binding protein, also known as CRIPT, takes part in the cytoskeletal anchoring of DLG4 in excitatory synapses.
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Synonyms
Cysteine-rich interactor of PDZ three, cysteine-rich PDZ-binding protein, Cysteine-rich interactor of PDZ3, postsynaptic protein CRIPT, HSPC139.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSIHHHHHH SSGLVPRGSH MGSMVCEKCE KKLGTVITPD TWKDGARNTT ESGGRKLNEN KALTSKKARF DPYGKNKFST CRICKSSVHQ PGSHYCQGCA YKKGICAMCG KKVLDTKNYK QTSV
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TGFB1 Human, HEKDescription:
Transforming Growth Factor-Beta 1 Human Recombinant, HEK
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Product # :
CYT-1260Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TGFB1 Human Recombinant produced in 293 cells is a glycosylated homodimer polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.0kDa. The TGFB1 is purified by proprietary chromatographic techniques.
Source
HEK 293 cells.
Formulation
Lyophilized from a sterile filtered solution containing TFA (0.1%).
Purity
Greater than 98.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 107 units/mg.
Citations
More Info
-
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized TGFB1 in sterile in 18MΩ-cm H2O at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
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Background
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HSV-1 gGDescription:
Herpes Simplex Virus-1 gG Recombinant
Product # :
HSV-224Price :
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Description
The E.Coli derived recombinant protein contains the HSV-1 gG immunodominant regions, 84-175 amino acids and fused to a GST-Tag at C-terminus.
Formulation
25mM Tris-HCl pH 7.2, 1mM EDTA, and 50% glycerol.
Purity
HSV-1 gG protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
-
Introduction
Entry of HSV into the host cell involves interactions of several viral glycoproteins with cell surface receptors. The virus particle is covered by an envelope which, when bound to specific receptors on the cell surface, will fuse with the cell membrane and create an opening, or pore, through which the virus enters the host cell. The sequential stages of HSV entry are analagous to those of other viruses. At first, complementary receptors on the virus and cell surface bring the two membranes into proximity. In an intermediate state, the two membranes begin to merge, forming a hemifusion state. Finally, a stable entry pore is formed through which the viral envelope contents are introduced to the host cell.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
HSV-1 gG protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Specificity
Immunoreactive with sera of HSV-infected individuals.
-
Purification Method
HSV-1 gG was purified by Sepharose-Derived Purification.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HNRNPA1 HumanDescription:
Heterogeneous Nuclear Ribonucleoprotein A1 Human Recombinant
Heterogeneous nuclear ribonucleoprotein A1, hnRNP A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1, HNRNPA1, HNRPA1, HNRPA1L3, hnRNP-A1.
Product # :
PRO-1038Price :
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Description
HNRNPA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a.) and having a molecular mass of 36.6kDa.HNRNPA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HNRNPA1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) is a member of the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPA1 is involved in the packing of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may control splice site selection. The HNRNPA1 protein may also have a role in HCV RNA replication. In addition, HNRNPA1 is believed to have a key role in the formation of specific myometrial protein species in parturition.
The hnRNP proteins have distinctive nucleic acid binding properties. HNRNPA1 has 2 repeats of quasi-RRM domains that bind to RNAs. HNRNPA1 is one of the most copious core proteins of hnRNP complexes and it is restricted to the nucleoplasm. The HNRNPA1 protein, along with other hnRNP proteins, is exported from the nucleus, most likely bound to mRNA, and is immediately re-imported. The M9 domain of HNRNPA1 functions as both a nuclear localization and nuclear export signal. -
Synonyms
Heterogeneous nuclear ribonucleoprotein A1, hnRNP A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1, HNRNPA1, HNRPA1, HNRPA1L3, hnRNP-A1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSKSESP KEPEQLRKLF IGGLSFETTD ESLRSHFEQW GTLTDCVVMR DPNTKRSRGF GFVTYATVEE VDAAMNARPH KVDGRVVEPK RAVSREDSQR PGAHLTVKKI FVGGIKEDTE EHHLRDYFEQ YGKIEVIEIM TDRGSGKKRG FAFVTFDDHD SVDKIVIQKY HTVNGHNCEV RKALSKQEMA SASSSQRGRS GSGNFGGGRG GGFGGNDNFG RGGNFSGRGG FGGSRGGGGY GGSGDGYNGF GNDGSNFGGG GSYNDFGNYN NQSSNFGPMK GGNFGGRSSG PYGGGGQYFA KPRNQGGYGG SSSSSSYGSG RRF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
DHFR HumanDescription:
Dihydrofolate Reductase Human Recombinant
Dihydrofolate reductase, DHFR, DHFRP1.
Product # :
ENZ-443Price :
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Description
DHFR Human Recombinant fused with a 20 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.6kDa.The DHFR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHFR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 2mM DTT and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >2000 pmol/min/ug is defined as the amount of enzyme that converts 1.0 pmole of dihydrofolic acid to tetrahydrofolic acid per minute at pH 6.5 at 25C.
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Introduction
Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes.
DHFR deficiency is associated with megaloblastic anemia.
DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid.
DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women. -
Synonyms
Dihydrofolate reductase, DHFR, DHFRP1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL VIMGKKTWFS IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL TEQPELANKV DMVWIVGGSS VYKEAMNHPG HLKLFVTRIM QDFESDTFFP EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF EVYEKND.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HSP27 Human, HisDescription:
Heat Shock Protein 27 Human Recombinant, His Tag
HSPB1, CMT2F, HMN2B, HSP27, HSP28, HSP25, Heat shock protein beta-1, Heat shock 27 kDa protein, Stress-responsive protein 27, SRP27, HS.76067, DKFZp586P1322.
Product # :
HSP-029Price :
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Description
Recombinant Human HSP-27 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-205 a.a.) and having a molecular mass of 24.9kDa. Hsp27 is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The HSP27 protein solution contains 20mM Tris-Hcl buffer, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HSP27 (also known as the Estrogen-Regulated 24K protein, and hsp 28) is a member of the mammalian small heat shock protein family. Hsp27 is expressed constitutively in many tissues and its expression is increased to high levels after various types of stress including elevated temperatures, toxic metals, drugs and oxidants. Also, Hsp27 is phosphorylated in vivo on three phosphorylation sites (Ser15, Ser78 and Ser82) by protein kinases including MAPKAP kinase 2 and the stress-activated protein kinase SAPK2 (p38).
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Synonyms
HSPB1, CMT2F, HMN2B, HSP27, HSP28, HSP25, Heat shock protein beta-1, Heat shock 27 kDa protein, Stress-responsive protein 27, SRP27, HS.76067, DKFZp586P1322.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD ETAAK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NDRG2 HumanDescription:
N-Myc Downstream Regulated 2 Human Recombinant
N-myc downstream-regulated gene 2 protein, NDR1-related protein NDR2, protein NDRG2, NDRG family member 2, cytoplasmic protein Ndr1, syld709613 protein, KIAA1248, SYLD.
Product # :
PRO-1198Price :
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Description
NDRG2 Human Recombinant produced in E. coli is a single polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 41.8 kDa.NDRG2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NDRG2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NDRG2 belongs to the N-myc downregulated gene family that is a part of the alpha/beta hydrolase superfamily. NDRG2 takes part in dendritic and neuronal cell differentiation and outgrowth and is found in large quantities in heart, dendritic cells, brain, salivary gland and skeletal muscle and in small quantities in kidney and liver. In Alzheimer Disease (AD)-affected patients NDRG2 is found in brain lesions and is believed to be related to the progression of AD.
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Synonyms
N-myc downstream-regulated gene 2 protein, NDR1-related protein NDR2, protein NDRG2, NDRG family member 2, cytoplasmic protein Ndr1, syld709613 protein, KIAA1248, SYLD.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAELQE VQITEEKPLL PGQTPEAAKT HSVETPYGSV TFTVYGTPKP KRPAILTYHD VGLNYKSCFQ PLFQFEDMQE IIQNFVRVHV DAPGMEEGAP VFPLGYQYPS LDQLADMIPC VLQYLNFSTI IGVGVGAGAY ILARYALNHP DTVEGLVLIN IDPNAKGWMD WAAHKLTGLT SSIPEMILGH LFSQEELSGN SELIQKYRNI ITHAPNLDNI ELYWNSYNNR RDLNFERGGD ITLRCPVMLV VGDQAPHEDA VVECNSKLDP TQTSFLKMAD SGGQPQLTQP GKLTEAFKYF LQGMGYMASS CMTRLSRSRT ASLTSAASVD GNRSRSRTLS QSSESGTLSS GPPGHTMEVS C.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
bNGF Human, CHODescription:
Beta-Nerve Growth Factor Human Recombinant, CHO
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Product # :
CYT-246Price :
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Shipped at Room temp
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Description
Nerve Growth Factor-beta Human Recombinant produced in CHO is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.The NGF-b is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells.
Formulation
The protein was lyophilized from a 0.2µm filtered solution in 20mM PB and 250mM NaCl, pH 7.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.Citations
More Info
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Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
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Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Nerve Growth Factor b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Nerve Growth Factor-beta should be stored at 4°C between 2-7 days and for future use below -18°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized NGF-b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Was analyzed by Mass spectrometry.
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Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 26.5kDa.
What is the source or expression system of B NGF Protein?
Chinese Hamster Ovary Cells.
What is the Purity of B NGF Protein?
B NGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of B NGF Protein?
The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.
What is the amino acid sequence of B NGF Protein?
B NGF Protein is composed from 118 amino acids.
What applications can B NGF Protein be used in?
B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for B NGF Protein?
The endotoxin level is minimal, B NGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.