Search: 1000 results found for "ephrin"

Description:

Erythropoietin clone PAT1C12AT, Mouse Anti Human

EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

Product # :

ANT-744

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
EPO is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of 4 alpha helical bundles. EPO is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
Synonyms
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Physical Appearance
Sterile filtered colorless solution.
Stability
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT1C12AT.
Type
Mouse Anti Human Monoclonal.
Purification Method
EPO antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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.

Description:

Eukaryotic Translation Initiation Factor 4H Human Recombinant

Eukaryotic translation initiation factor 4H, eIF-4H, Williams-Beuren syndrome chromosomal region 1 protein, EIF4H, KIAA0038, WBSCR1, WSCR1.

Product # :

PRO-1114

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Description

EIF4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a) and having a molecular mass of 29.9kDa.EIF4H is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EIF4H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Eukaryotic translation initiation factor 4H (EIF4H) is a 248 amino acid protein which localizes to the perinuclear region of the cytoplasm and is expressed as 2 isoforms, termed short and long. EIF4H functions to stimulate the initiation of protein synthesis at the level of mRNA employment. EIF4H stimulates the RNA-dependent ATP hydrolysis catalyzed by EIF4A and EIF4B. EIF4H gene defects linked to Williams- Beuren syndrome (WBS), a rare developmental disorder characterized by cardiovascular and musculo-skeletal abnormalities and caused by the deletion of contiguous genes at 7q11.23.
Synonyms
Eukaryotic translation initiation factor 4H, eIF-4H, Williams-Beuren syndrome chromosomal region 1 protein, EIF4H, KIAA0038, WBSCR1, WSCR1.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMADFDT YDDRAYSSFG GGRGSRGSAG GHGSRSQKEL PTEPPYTAYV GNLPFNTVQG DIDAIFKDLS IRSVRLVRDK DTDKFKGFCY VEFDEVDSLK EALTYDGALL GDRSLRVDIA EGRKQDKGGF GFRKGGPDDR GMGSSRESRG GWDSRDDFNS
GFRDDFLGGR GGSRPGDRRT GPPMGSRFRD GPPLRGSNMD FREPTEEERA QRPRLQLKPR TVATPLNQVA NPNSAIFGGA RPREEVVQKE QE.

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.

Description:

E-Cadherin Human Recombinant, Sf9

Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-1.

Product # :

PRO-2265

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Description

CDH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 694 amino acids (24-709a.a.) and having a molecular mass of 76.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70kDa). CDH1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CDH1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. It plays an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Numerous studies have demonstrated that reduction and/or loss of Ecadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis.
Synonyms
Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-1.
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.
Amino Acid Sequence
EPEPCHPGFD AESYTFTVPR RHLERGRVLG RVNFEDCTGR QRTAYFSLDT RFKVGTDGVI TVKRPLRFHN PQIHFLVYAW DSTYRKFSTK VTLNTVGHHH RPPPHQASVS GIQAELLTFP NSSPGLRRQK RDWVIPPISC PENEKGPFPK NLVQIKSNKD KEGKVFYSIT GQGADTPPVG VFIIERETGW LKVTEPLDRE RIATYTLFSH AVSSNGNAVE DPMEILITVT DQNDNKPEFT QEVFKGSVME GALPGTSVME VTATDADDDV NTYNAAIAYT ILSQDPELPD KNMFTINRNT GVISVVTTGL DRESFPTYTL VVQAADLQGE GLSTTATAVI TVTDTNDNPP IFNPTTYKGQ VPENEANVVI TTLKVTDADA PNTPAWEAVY TILNDDGGQF VVTTNPVNND GILKTAKGLD FEAKQQYILH VAVTNVVPFE VSLTTSTATV TVDVLDVNEA PIFVPPEKRV EVSEDFGVGQ EITSYTAQEP DTFMEQKITY RIWRDTANWL EINPDTGAIS TRAELDREDF EHVKNSTYTA LIIATDNGSP VATGTGTLLL ILSDVNDNAP IPEPRTIFFC ERNPKPQVIN IIDADLPPNT SPFTAELTHG ASANWTIQYN DPTQESIILK PKMALEVGDY KINLKLMDNQ NKDQVTTLEV SVCDCEGAAG VCRKAQPVEA GLQIPALEHH HHHH.

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.

Description:

Elcatonin

Product # :

HOR-302

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Description

Elcatonin Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3363.2 Dalton and a Molecular formula of C148H244N42O47.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 93.3% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.

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Introduction
Elcatonin is a Calcitonin derivative which is transformed from eel´s calcitonin by changing the S-S bond into the stable C-N bond. It inhibits the absorption and autolysis of bones, thus leads to blood calcium descending. In addition, it inhibits the bone salts dissolving and transferring and promotes the excretion of calcium and phosphorus in urine. Meanwhile, it inhibits renal tubules reabsorbing calcium, phosphorus and sodium and keeps blood calcium at normal level. It is mainly used for remitting or eliminating the pain caused by Osteoporosis.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Elcatonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Elcatonin 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.
Solubility
It is recommended to reconstitute the lyophilized Elcatonin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.
Background
What is the molecular weight/Mw of ELCATONIN Protein?
ELCATONIN Protein has a total Mw of 3.36kDa.

What is the Purity of ELCATONIN Protein?
ELCATONIN Protein is > 93.3% pure as determined by SDS-PAGE.

What is the Biological Activity of ELCATONIN Protein?
Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.

What is the amino acid sequence of ELCATONIN Protein?
Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.

What applications can ELCATONIN Protein be used in?
ELCATONIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ELCATONIN Protein?
The endotoxin level is minimal, ELCATONIN Protein was purified using conventional chromatography techniques.

Who supplies ELCATONIN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of ELCATONIN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Darbepoetin-Alpha Human Recombinant

Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

Product # :

CYT-1263

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Description

Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells(CHO).

Formulation

Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

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Introduction
Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.
Synonyms
NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Darbepoetin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Darbepoetin 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.
Solubility
It is recommended to reconstitute the lyophilized Darbepoetin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.
Background
What is the molecular weight/Mw of DARBEPOETIN Protein?
DARBEPOETIN Protein has a total Mw of 38.5kDa.

What is the source or expression system of DARBEPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).

What is the Purity of DARBEPOETIN Protein?
DARBEPOETIN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of DARBEPOETIN Protein?
The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

What is the amino acid sequence of DARBEPOETIN Protein?
APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD

What applications can DARBEPOETIN Protein be used in?
DARBEPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for DARBEPOETIN Protein?
The endotoxin level is minimal, DARBEPOETIN 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.

Description:

Epidermal Growth Factor Receptor Clone PAT2H8AT, Mouse Anti Human

ERBB, ERBB1, Epidermal growth factor receptor, HER1, PIG61, epidermal growth factor receptor, Urogastrone, Proto-oncogene c-ErbB-1, Oncogene ERBB, Cell proliferation inducing protein 61, Cell growth inhibiting protein 40, Avian erythroblastic leukemia viral (verbb) oncogene homolog.

Product # :

ANT-751

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Epidermal growth factor receptor or EGFR or Erb-1 is a membranal protein that acts as a receptor for the extracellular EGF proteins family. This protein is a part of a family of receptors called ErbB family which are all tyrosine kinases receptors. Mutations in the gene of this receptors can cause cancer.
Synonyms
ERBB, ERBB1, Epidermal growth factor receptor, HER1, PIG61, epidermal growth factor receptor, Urogastrone, Proto-oncogene c-ErbB-1, Oncogene ERBB, Cell proliferation inducing protein 61, Cell growth inhibiting protein 40, Avian erythroblastic leukemia viral (verbb) oncogene homolog.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human EGFR mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EGFR amino acids 424-605 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT2H8AT.
Applications
EGFR antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
EGFR antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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.

Description:

Epidermal Growth Factor Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-217

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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.

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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.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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.
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.
Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
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.

Description:

Eukaryotic Translation Initiation Factor 3K (50-94 a.a.) Human Recombinant

PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.

Product # :

PRO-2833

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Description

The EIF3KHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The EIF3KHis-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 45 amino acid residues of the EIF3KHuman, 50-94 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized EIF3Kat -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.
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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Eukaryotic Translation Initiation Factor 3K (EIF3K) is a part of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a few other subunits of the 40S ribosomal subunit and eIF3. EIF3K is found both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4. EIF3K is conserved among high eukaryotes, including mammals, plants and insects and is expressed in human tissues.

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.

Description:

Eukaryotic Translation Initiation Factor 4E-Binding Protein 2 Human Recombinant

Eukaryotic Translation Initiation Factor 4E Binding Protein 2, 4E-BP2, eIF4E-binding protein 2, 4EBP2, PHASII, phosphorylated.

Product # :

PRO-176

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Description

EIF4EBP2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140amino acids (1-120a.a.) and having a molecular mass of 15.1 kDa. EIF4EBP2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EIF4EBP2 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
EIF4EBP2 belongs to the eukaryotic translation initiation factor 4E binding protein family. Even though EIF4EBP2 protein binds eIF4E and inhibits translation initiation, growth factors can release this inhibition by a phosphorylation-dependent disruption. EIF4EBP2 mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase pathway. Regulation of this protein is associated to cell proliferation, cell differentiation and viral infection.
Synonyms
Eukaryotic Translation Initiation Factor 4E Binding Protein 2, 4E-BP2, eIF4E-binding protein 2, 4EBP2, PHASII, phosphorylated.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSSAGSGHQ PSQSRAIPTR TVAISDAAQL PHDYCTTPGG TLFSTTPGGT RIIYDRKFLL DRRNSPMAQT PPCHLPNIPG VTSPGTLIED SKVEVNNLNN LNNHDRKHAV GDDAQFEMDI.

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.

Description:

Egl Nine Homolog 3 Human Recombinant

Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.

Product # :

PRO-1143

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Description

EGLN3 Human Recombinant produced in E. coli is a single polypeptide chain containing 263 amino acids (1-239) and having a molecular mass of 29.8 kDa.EGLN3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EGLN3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 300mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.
Synonyms
Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED

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.

Description:

Erythropoietin-Alpha Fc-Chimera Human Recombinant

EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

Product # :

CYT-325

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Description

Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.

Source

Chinese Hamster Ovary Cells(CHO).

Formulation

Each mg of lyophilized powder contains 1x PBS pH-7.4.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 10⁵ IU/mg.

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Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
Synonyms
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Erythropoietin-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha 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.
Solubility
It is recommended to reconstitute the lyophilized Erythropoietin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 140kDa.

What is the source or expression system of EPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).

What is the Purity of EPOETIN Protein?
EPOETIN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EPOETIN Protein?
The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.

What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN 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.

Description:

Erythropoietin-alpha Human Recombinant, Sf9

Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.

Product # :

CYT-934

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Description

Erythropoietin-alpha Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 174 amino acids (28-193a.a.) and having a molecular mass of 19.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPO-a is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

EPO a protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED₅₀ for this effect is ≤ 0.5 ng/ml.

sds-page

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Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
Synonyms
Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.
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.
Amino Acid Sequence
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.
Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 19.5kDa.

What is the source or expression system of EPOETIN Protein?
Sf9, Insect cells.

What is the Purity of EPOETIN Protein?
EPOETIN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EPOETIN Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is ≤ 0.5 ng/ml.

What is the amino acid sequence of EPOETIN Protein?
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN 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.

Description:

Hemopexin Human Recombinant

Hemopexin, Beta-1B-glycoprotein, HPX, Haemopexin.

Product # :

PRO-1869

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Description

Hemopexin Human Recombinant produced in E. coli is. a single polypeptide chain containing 462 amino acids (24-462) and having a molecular mass of 51.7kDa. Hemopexin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Hemopexin solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Hemopexin (or haemopexin) is a plasma protein that binds heme with the highest affinity of any known protein. Hemopexin is generally expressed in liver, and belongs to acute phase reactants, the synthesis of which is induced after inflammation. Heme is potentially very toxic because of its ability to intercalate into lipid membrane and to generate hydroxyl radicals. Hemopexin’s function of scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin defends the body from the oxidative damage that free heme can cause. Additionally, hemopexin discharges its bound ligand for internalisation upon interacting with a specific receptor located on the surface of liver cells. This hemopexin function is in order to preserve the body's iron. Hemopexin’s levels in the serum are an indication of how much heme is present in the blood. Low Hemopexin levels show that there is a lot of it in the serum. For that reason, low hemopexin levels indicate that there has been consid
Synonyms
Hemopexin, Beta-1B-glycoprotein, HPX, Haemopexin.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN GTGHGNSTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG TPHGIILDSV DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH EKVDGALCME KSLGPNSCSA NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC TH.

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.

Description:

Eukaryotic Translation Initiation Factor 2 Subunit 1 Alpha Human Recombinant

Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.

Product # :

PRO-845

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Description

EIF2S1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-315 a.a.) and having a molecular mass of 38.2 kDa. The EIF2S1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

0.5mg/ml solution containing 20mM Tris-HCl pH-8, 0.1M NaCl & 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
EIF2S1 participates in the premature steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA which binds to a 40S ribosomal subunit, followed by mRNA binding to create a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 should exchange with GTP by way of a reaction catalyzed by eIF-2B.
Synonyms
Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP SILDSLDLNE DEREVLINNI NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ENMPIKINLI APPRYVMTTT TLERTEGLSV LSQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQM ERLERENAEV DGDDDAEEME AKAED

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.

Description:

Eukaryotic Translation Initiation Factor 3J Human Recombinant

Eukaryotic translation initiation factor 3 subunit J, Eukaryotic translation initiation factor 3 subunit 1, eIF-3-alpha, eIF3 p35, EIF3J, EIF3S1, eIF3-alpha.

Product # :

PRO-970

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Description

EIF3J Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (70-258) and having a molecular mass of 24kDa (Molecular weight on SDS-PAGE will appear higher).EIF3J is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EIF3J solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Eukaryotic translation initiation factor 3 subunit J (EIF3J) is a member of the EIF-3 subunit J family. EIF3 has a crucial role in binding of initiator methionyl-tRNA and mRNA to the 40S ribosomal subunit to produce the 40S initiation complex. EIF3J binds to the aminoacyl (A) site and mRNA access channel of the 40S subunit, setting EIF3J directly in the ribosomal decoding center. In addition, EIF3J interacts with eIF1A and reduces 40S subunit affinity for mRNA. An elevated affinity for mRNA is restored upon enlistment of initiator tRNA, despite the fact EIF3J remains in the mRNA-binding cleft in the presence of tRNA.
Synonyms
Eukaryotic translation initiation factor 3 subunit J, Eukaryotic translation initiation factor 3 subunit 1, eIF-3-alpha, eIF3 p35, EIF3J, EIF3S1, eIF3-alpha.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKISEKKKIA EKIKEKERQQ KKRQEEIKKR LEEPEEPKVL TPEEQLADKL RLKKLQEESD LELAKETFGV NNAVYGIDAM NPSSRDDFTE FGKLLKDKIT QYEKSLYYAS FLEVLVRDVC ISLEIDDLKK ITNSLTVLCS EKQKQEKQSK AKKKKKGVVP GGGLKATMKD DLADYGGYDG GYVQDYEDFM.

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.

Description:

Resistin Human Recombinant, HEK

RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.

Product # :

CYT-1183

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Description

Resistin Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (19-108 a.a) containing 96 amino acids and having a molecular mass of 10.3 kDa.Resistin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

Resistin protein (1mg/ml) contains 20% glycerol and 20mM Sodium citrate (pH3.0).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis.Resistin blocks insulinstimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of lowdensity lipoprotein (LDL), increasing the risk of heart disease.
Synonyms
RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.
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.
Amino Acid Sequence
KTLCSMEEAI NERIQEVAGS LIFRAISSIG LECQSVTSRG DLATCPRGFA VTGCTCGSAC GSWDVRAETT CHCQCAGMDW TGARCCRVQP 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.

Description:

Decorin Human Recombinant

Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

Product # :

PRO-1583

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Description

DCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (31-359 a.a) and having a molecular mass of 38.6kDa.DCN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DCN protein solution (0.25mg/ml) containing 20mM Tris pH 8.0 and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDEASGIGPE VPDDRDFEPS LGPVCPFRCQ CHLRVVQCSDLGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK VSPGAFTPLVKLERLYLSKN QLKELPEKMP KTLQELRAHE NEITKVRKVT FNGLNQMIVI ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD GNKISRVDAA SLKGLNNLAKLGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA EHKYIQVVYL HNNNISVVGSSDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK.

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.

Description:

Avidin

Avidin, AVD, AVID.

Product # :

PRO-500

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Description

Avidin is a glycosylated polypeptide chain having a molecular mass of 68kDa and containing 4 subunits each with a binding site for biotin. The Avidin is purified by affinity chromatographic techniques.The purification procedure ensures minimal contamination by other proteins or DNA.The resulting high activity and purity of the product gives very low non-specific binding (NSB).

Source

Hen's egg white.

Biological Activity

15.0 units/mg protein, 1 unit binds 1µg biotin.

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Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) each of which can bind to biotin with a high degree of affinity and specificity. Avidin molecular weight in its tetrameric form is estimated to be between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of four to five mannose and three N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.
Synonyms
Avidin, AVD, AVID.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Avidin 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.
Solubility
It is recommended to reconstitute the lyophilized Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.

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.

Description:

Epitalon

Product # :

HOR-031

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Description

Epithalon Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 390.35 Dalton and a Molecular formula of C14H22N4O9.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epithalon although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epithalon 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.
Solubility
It is recommended to reconstitute the lyophilized Epithalon in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Ala-Glu-Asp-Gly-OH .
Background
Epitalon, also known as Epithalon, is a synthetic tetrapeptide that has been a focal point in the field of aging and longevity research. This peptide, consisting of four amino acids, is derived from the pineal gland and has been associated with a variety of biological effects, most notably its potential role in extending the lifespan of cells.
Epitalon's primary function is its interaction with telomeres, the protective caps at the ends of chromosomes that shorten as cells divide. By stimulating the production of telomerase, an enzyme that can repair and lengthen telomeres, Epitalon may slow down the aging process at a cellular level.
Numerous studies have explored the potential of Epitalon in extending the lifespan of organisms. For instance, Khavinson and colleagues (2003) found that Epitalon increased the lifespan of fruit flies, while Anisimov et al. (2003) reported similar results in mice. These findings suggest that Epitalon could potentially have similar effects in humans.
Epitalon has also been studied for its role in regulating circadian rhythms. Korkushko et al. (2011) found that Epitalon could restore disrupted circadian rhythms in elderly people, suggesting potential applications in sleep disorders and other conditions related to circadian rhythm disruption.
Beyond its potential role in aging and longevity, Epitalon has been explored for its potential therapeutic applications. Anisimov et al. (2011) found that Epitalon could reduce the incidence of spontaneous tumors in mice, suggesting potential applications in cancer prevention.
While research on Epitalon is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of Epitalon in humans. However, the existing body of research suggests that Epitalon could be a promising tool in the fight against aging and age-related diseases.

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.

Description:

Eukaryotic Translation Initiation Factor 1 Human Recombinant

A121, EIF-1, EIF1A, ISO1, SUI1, Eukaryotic translation initiation factor 1, eIF1, Protein translation factor SUI1 homolog, Sui1iso1, EIF1.

Product # :

PRO-773

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Description

EIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-113 a.a.) and having a molecular weight of 16.9kDa.The EIF1 is fused to 37 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EIF1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
EIF1 is important for scanning and plays a role in initiation site selection. EIF1 promotes the assembly of 48S ribosomal at the authentic initiation codon of a conventional capped mRNA.
Synonyms
A121, EIF-1, EIF1A, ISO1, SUI1, Eukaryotic translation initiation factor 1, eIF1, Protein translation factor SUI1 homolog, Sui1iso1, EIF1.
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.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWAGSMSA IQNLHSFDPF ADASKGDDLL PAGTEDYIHI RIQQRNGRKT LTTVQGIADD YDKKKLVKAF KKKFACNGTV IEHPEYGEVI QLQGDQRKNI CQFLVEIGLA KDDQLKVHGF.

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.

Description:

Eukaryotic Translation Initiation Factor 5A2 Human Recombinant

eIF-5A-2, EIF-5A2, eIF5AII, Eukaryotic translation initiation factor 5A-2, Eukaryotic initiation factor 5A isoform 2, EIF5A2.

Product # :

PRO-846

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

EIF5A2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-153 a.a.) and having a molecular mass of 18.9 kDa. The EIF5A2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EIF5A2 Human solution containing 20mM Tris-HCl pH-8 & 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
EIF5A2 is part of the eukaryotic initiation factor 5A subfamily, is an vital protein strongly linked to cellular polyamine homeostasis. EIF5A2 promotes the formation of the first peptide bond during the initial stage of protein synthesis. EIF5A2 is the single eukaryotic protein to have a hypusine residue, which is a post-translational modification of a lysine by the addition of a butylamino group.
Synonyms
eIF-5A-2, EIF-5A2, eIF5AII, Eukaryotic translation initiation factor 5A-2, Eukaryotic initiation factor 5A isoform 2, EIF5A2.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MADEIDFTTG DAGASSTYPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG IDIFTGKKYE DICPSTHNMD VPNIKRNDYQ LICIQDGYLS LLTETGEVRE DLKLPEGELG KEIEGKYNAG EDVQVSVMCA MSEEYAVAIK PCK.

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.

Description:

Ghrelin Human

Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.

Product # :

HOR-297

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Ghrelin Human contains 28 amino acids and a total molecular mass of 3370.9 Dalton and a molecular formula of C149H249N47O42.The GHRL is purified by proprietary chromatographic techniques.

Formulation

GHRL was lyophilized without additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Physical Appearance
Sterile Filtered Yellowish lyophilized (freeze-dried) powder that may appear as a gel form.
Stability
Store the lyophilized Ghrelin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted GHRL can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add deionized water to a working concentration approximately 0.5mg/1ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
Gly-Ser-Ser(n-octanoyl)-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH.
Background
What is the molecular weight/Mw of GHRL Protein?
GHRL Protein has a total Mw of 3.37kDa.

What is the Purity of GHRL Protein?
GHRL Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GHRL Protein?
The biological functionality of GHRL Protein will be determined in the future.

What is the amino acid sequence of GHRL Protein?
Gly-Ser-Ser(n-octanoyl)-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH.

What applications can GHRL Protein be used in?
GHRL Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GHRL Protein?
The endotoxin level is minimal, GHRL Protein was purified using conventional chromatography techniques.

Who supplies GHRL that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of GHRL?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Epidermal Growth Factor Rat

Urogastrone, URG, EGF.

Product # :

CYT-556

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Adult Male Rat Submandibular Glands.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

Purity

Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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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.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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.
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.
Background
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential
Abstract:
This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.
Protein Expression and Purification:
The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.
Cellular Signaling Pathways and Responses:
In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Structural Modeling:
Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.
Therapeutic Implications and Future Prospects:
EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.
Challenges and Future Directions:
Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.
Conclusion:
A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.15kDa.

What is the source or expression system of EGF RAT Protein?
Adult Male Rat Submandibular Glands.

What is the Purity of EGF RAT Protein?
EGF RAT Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF RAT Protein?
The biological functionality of EGF RAT Protein will be determined in the future.

What is the amino acid sequence of EGF RAT Protein?
EGF RAT Protein is composed from 53 amino acids.

What applications can EGF RAT Protein be used in?
EGF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT 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.

Description:

HB-EGF Human Recombinant

HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

Product # :

CYT-119

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 10⁶units/mg.

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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
Synonyms
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-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.
Solubility
It is recommended to reconstitute the lyophilized Human HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.9kDa.

What is the source or expression system of HB-EGF Protein?
Escherichia Coli.

What is the Purity of HB-EGF Protein?
HB-EGF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of HB-EGF Protein?
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

What is the amino acid sequence of HB-EGF Protein?
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.

What applications can HB-EGF Protein be used in?
HB-EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-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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