Search results
1000 results found for “vegf protein”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
SUMO3 HumanDescription:
Small Ubiquitin-Related Modifier 3 Human Recombinant
SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.
Product # :
PRO-267Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SUMO3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (1-92a.a.) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).SUMO3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SUMO3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl,1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
SUMO3 belongs to the SUMO protein family and operates like ubiquitin. Nevertheless, unlike ubiquitin that targets proteins for degradation, SUMO3 protein takes part in several cellular processes, like nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO3 regulates amyloid beta generation and is crucial in the onset or progression of Alzheimer’s disease.
-
Synonyms
SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.
-
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 MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GG
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 :
CNTF Human, HisDescription:
Ciliary Neurotrophic Factor Human Recombinant, His Tag
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-573Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 1-200) containing a total of 220 amino acids and having a molecular mass of 25kDa. The CNTF protein is fused to a 20 aa His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNTF protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH-8 and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
-
Physical Appearance
Sterile Filtered colorless 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 MAFTEHSPLT PHRRDLCSRS IWLARKIRSDLTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
-
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 25kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
The biological functionality of CNTF Protein will be determined in the future.
What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSDLTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF 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.
- View Data Sheet
Name :
CRK HumanDescription:
V-crk Sarcoma Virus CT10 Oncogene Human Recombinant
Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.
Product # :
PRO-275Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CRK Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids (1-204 a.a.) and having a molecular mass of 25kDa. The CRK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRK solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CRK belongs to the signaling adapter protein family which binds to several tyrosine-phosphorylated proteins. CRK is involved in many cellular processes such as apoptosis, proliferation, and differentiation. CRK has a modular domain architecture consisting of an SH2 followed by two SH3 domains (src-homology domains). The N-terminal SH2 domain of the CRK protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation.
-
Synonyms
Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.
-
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).Please prevent freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVSR SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL IGGR.
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 :
TFPI Human, Sf9Description:
Tissue Factor Pathway Inhibitor Human Recombinant, Sf9
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
Product # :
PRO-2441Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TFPI Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 285 amino acids (29-304a.a.) and having a molecular mass of 33kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TFPI is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TFPI protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
TFPI is a protease inhibitor which controls the tissue factor (TF)-dependent pathway of blood coagulation. The coagulation process starts with the creation of a factor VIIa-TF complex, that proteolytically triggers additional proteases (factors IX and X) and eventually results in a fibrin clot. TFPI inhibits the activated factor X and VIIa-TF proteases in an autoregulatory loop. TFPI is glycosylated and predominantly located in the vascular endothelium and plasma in both free forms and complexed with plasma lipoproteins. A number of alternatively spliced transcript variants of this gene have are known, however the full-length nature of several of these variants were not yet established.
-
Synonyms
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
-
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
ADPDSEEDEE HTIITDTELP PLKLMHSFCA FKADDGPCKA IMKRFFFNIF TRQCEEFIYG GCEGNQNRFE SLEECKKMCT RDNANRIIKT TLQQEKPDFC FLEEDPGICR GYITRYFYNN QTKQCERFKY GGCLGNMNNF ETLEECKNIC EDGPNGFQVD NYGTQLNAVN NSLTPQSTKV PSLFEFHGPS WCLTPADRGL CRANENRFYY NSVIGKCRPF KYSGCGGNEN NFTSKQECLR ACKKGFIQRI SKGGLIKTKR KRKKQRVKIA YEEIFVKNMH HHHHH.
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 :
SNURF HumanDescription:
SNRPN Upstream Reading Frame Human Recombinant
SNRPN Upstream Reading Frame Protein.
Product # :
PRO-1849Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SNURF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (1-71) and having a molecular mass of 10.8 kDa. SNURF is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The SNURF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
SNURF is an extremely basic protein restricted to the nucleus. The evolutionarily reserved open reading frame is located on a bicistronic transcript which has a downstream ORF encoding the small nuclear ribonucleoprotein polypeptide N. The first three exons of the transcript are exploited by the upstream coding region which is known as an imprinting center. The full-length nature of these transcripts is yet to be determined but multiple transcription initiation sites have been identified and large scale alternative splicing takes place in the 5' untranslated region. An alternate exon which substitutes for exon 4 and leads to a truncated, monocistronic transcript was identified. Deletion or alternative splicing produced by a translocation event in the 5' UTR or coding region of this gene results in Prader-Willi syndrome or Angelman syndrome because of parental imprint switch failure.
-
Synonyms
SNRPN Upstream Reading Frame Protein.
-
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 MGSMERARDR LHLRRTTEQH VPEVEVQVKR RRTASLSNQE CQLYPRRSQQ QQVPVVDFQA ELRQAFLAET PRGG
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 :
METRN MouseDescription:
Meteorin Mouse Recombinant
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
Product # :
PRO-2241Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
METRN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
-
Synonyms
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
-
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
GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD 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 :
CCN1 HumanDescription:
Cysteine-Rich Angiogenic Inducer 61 Human Recombinant
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Product # :
CYT-164Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CYR61 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids and having a molecular mass of 39.5kDa.The CYR61 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2m filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.More Info
-
Introduction
CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
-
Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized CYR61 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD -
Background
Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis
Abstract:
Cysteine-rich angiogenic inducer 61 (CYR61) is an important extracellular matrix-associated protein that plays a significant role in angiogenesis and cell adhesion. This research paper provides a comprehensive analysis of human recombinant CYR61, focusing on its production, characterization, and potential applications in regulating angiogenesis. The paper discusses the significance of CYR61 in physiological and pathological angiogenesis, including wound healing, tumor development, and cardiovascular diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYR61 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYR61 and its utility as a research tool and a potential regulator of angiogenesis.Introduction:
Cysteine-rich angiogenic inducer 61 (CYR61) is an extracellular matrix-associated protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. Human recombinant CYR61, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.Production and Characterization:
Recombinant CYR61 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYR61.Role in Angiogenesis:
CYR61 is involved in various aspects of angiogenesis, including endothelial cell proliferation, migration, and tube formation. It interacts with integrins and other cell surface receptors to modulate signaling pathways involved in angiogenic processes. Recombinant CYR61 serves as a valuable tool for studying the mechanisms underlying angiogenesis and exploring its potential as a therapeutic target.Therapeutic Implications:
The dysregulation of angiogenesis is associated with several pathological conditions, including cancer, cardiovascular diseases, and chronic wounds. Recombinant CYR61 has shown promise as a potential regulator of angiogenesis and a therapeutic agent. It can be used to promote or inhibit angiogenesis, depending on the specific context. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYR61 in various diseases, including cancer and ischemic disorders.Conclusion:
Human recombinant CYR61 is a valuable research tool and a potential regulator of angiogenesis. Its production, characterization, and applications in modulating angiogenic processes contribute to our understanding of angiogenesis and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYR61 offer promising prospects for improving outcomes in cancer, cardiovascular diseases, and wound healing.What is the molecular weight/Mw of CCN1 Protein?
CCN1 Protein has a total Mw of 39.5kDa.
What is the source or expression system of CCN1 Protein?
Escherichia Coli.
What is the Purity of CCN1 Protein?
CCN1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCN1 Protein?
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.
What is the amino acid sequence of CCN1 Protein?
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD
What applications can CCN1 Protein be used in?
CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 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.
- View Data Sheet
Name :
NOV Human, HEKDescription:
Nephroblastoma Overexpressed Human Recombinant, HEK
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Product # :
CYT-1032Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 33-357) containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa (calculated).
Source
HEK293 cells.
Formulation
NOV filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
-
Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
-
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 one week 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. NOV is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEVSDS SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH H.
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 :
SCGB2A2 Human, HEKDescription:
Mammaglobin-A Human Recombinant, HEK
Mammaglobin-A, Mammaglobin-1, Secretoglobin family 2A member 2, SCGB2A2, MGB1, UGB2, MGC71974.
Product # :
PRO-2038Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Mammaglobin-A Human Recombinant (Fc Chimera) produced in HEK cells is a single, glycosylated, polypeptide chain (Gly19-Phe93) containing a total of 321 amino acids, having a calculated molecular mass of 36.3kDa. The SCGB2A2 protein is fused to a 2 aa C-terminal linker, a 6 aa C-terminal His tag, a 7 aa TEV site and a 231 aa Human IgG1 fragment (Pro100-Lys330).
Source
HEK 293.
Formulation
SCGB2A2 was filtered (0,4µm) and lyophilized from 0.5mg/ml in PBS buffer and 5% (w/v) Threalose pH 7.4
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
The mammaglobin gene was first identified using a differential screening approach directed at the isolation of novel, human breast cancer-associated genes. Mammaglobin encodes a 10 kDa glycoprotein and is distantly relaetd to a family of epithelial secretory proteins that includes rat estramustine-binding protein/prostatein and human Clara cell 10 kDa protein (CC10)/uteroglobin. Mammaglobin, a mammary-specific member of the uterglobin family, is known to be overexpressed in human breast cancer. Studies suggest that mammaglobin is one of the first relatively mammary-specific and mammary-sensitive markers (85%). Mammaglobin may be valuable used in a panel with BRST-2 (GCDFP-15) and ER in evaluating tumors of unknown primary sites.
SCGB2A2 (the mammaglobin gene) is located on chromosome 11, at locus 11q13. SCGB2A2 is member of the secretoglobin superfamily of which is a group of small dimeric secreted and sometimes glycosylated proteins. Expressed mainly in mucosa, secretoglobins appear to be involved in cell signalling, immune response, chemotaxis, and might also serve as transporters for steroid hormones in humans. -
Synonyms
Mammaglobin-A, Mammaglobin-1, Secretoglobin family 2A member 2, SCGB2A2, MGB1, UGB2, MGC71974.
-
Physical Appearance
Sterile filtered lyophilized 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 5 days.
-
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.
-
Amino Acid Sequence
GSGCPLLENV ISKTINPQVS KTEYKELLQE FIDDNATTNA IDELKECFLN QTDETLSNVE VFMQLIYDSS LCDLF KLENL YFQGPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
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 :
EIF2S1 HumanDescription:
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-845Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
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.
More Info
-
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.
- View Data Sheet
Name :
HOXB13 HumanDescription:
Homeobox B13 Human Recombinant
Homeobox B13, Homeobox Protein Hox-B13, PSGD.
Product # :
PRO-1765Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HOXB13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (1-284 a.a) and having a molecular mass of 33.1kDa.HOXB13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HOXB13 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
HOXB13 is a transcription factor and a member of the homeobox gene family which are extremely conserved in vertebrates and vital for vertebrate embryonic development. HOXB13 is involved in fetal skin development and cutaneous regeneration. In mice, a similar gene displayed temporal and spatial colinearity in the main body axis of the embryo, however it was not expressed in the secondary axes, implying that it has a roles in body patterning along the axis.
-
Synonyms
Homeobox B13, Homeobox Protein Hox-B13, PSGD.
-
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).Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEPGNYA TLDGAKDIEG LLGAGGGRNL VAHSPLTSHP AAPTLMPAVN YAPLDLPGSA EPPKQCHPCP GVPQGTSPAP VPYGYFGGGY YSCRVSRSSL KPCAQAATLA AYPAETPTAG EEYPSRPTEF AFYPGYPGTY QPMASYLDVS VVQTLGAPGE PRHDSLLPVD SYQSWALAGG WNSQMCCQGE QNPPGPFWKA AFADSSGQHP PDACAFRRGR KKRIPYSKGQ LRELEREYAA NKFITKDKRR KISAATSLSE RQITIWFQNR RVKEKKVLAK VKNSATP
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 :
SLAMF1 Human, Sf9Description:
SLAMF1 Human Recombinant, Sf9
Signaling lymphocytic activation molecule, CDw150, IPO-3, CD150, SLAMF1, SLAM.
Product # :
PRO-2393Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SLAMF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 226 amino acids (21-237a.a.) and having a molecular mass of 25.3kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).SLAMF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SLAMF1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
SLAMF1 is a member of the immunoglobulin gene superfamily and is involved in T-cell stimulation. The SLAMF1 protein is constitutively expressed on peripheral blood memory T cells, T-cell clones, immature thymocytes, and a fraction of B cells, and is swiftly induced on naive T cells after activation. There are probably 2 modes of SLAM signaling: one in which the inhibitor SH2D1A serves as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction functions.
-
Synonyms
Signaling lymphocytic activation molecule, CDw150, IPO-3, CD150, SLAMF1, SLAM.
-
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
ADPASYGTGG RMMNCPKILR QLGSKVLLPL TYERINKSMN KSIHIVVTMA KSLENSVENK IVSLDPSEAG PPRYLGDRYK FYLENLTLGI RESRKEDEGW YLMTLEKNVS VQRFCLQLRL YEQVSTPEIK VLNKTQENGT CTLILGCTVE KGDHVAYSWS EKAGTHPLNP ANSSHLLSLT
LGPQHADNIY ICTVSNPISN NSQTFSPWPG CRTDPSETKP 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 :
S100A8 HumanDescription:
S100 Calcium Binding Protein A8 Human Recombinant
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
Product # :
PRO-800Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
S100A8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (1-93 a.a.) and having a molecular mass of 10.8 kDa. The S100A8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The S100A8 solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
-
Synonyms
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
-
Physical Appearance
Sterile Filtered clear 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
MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.
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
Description:
Hepatocyte Growth Factor Human Recombinant
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.
Product # :
CYT-244Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Hepatocyte Growth Factor Human Recombinant produced in Baculovirus is a heterodimer, non-glycosylated, polypeptide chain containing 697 a.a and having a total molecular mass of 78.0 KDa.The HGF is purified by proprietary chromatographic techniques.
Source
Insect cells.
Formulation
The sterile protein powder (1 mg/ml) is lyophilized from a solution containing 50mM acetic acid.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity was assayed for scattering activity in the MDCK cell assay. The ED50 for this effect is typically at 2.0-5.0 ng/ml.
More Info
-
Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
-
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Hepatocyte Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF 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 Hepatocyte Growth Factor in 50mM acetic acid to a concentration not less than 100µg/ml. Further dilutions should be made using buffer containing protein.
-
Amino Acid Sequence
QRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCK
AFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYENKDYIRNCIIGKGRSYKGT
VSITKSGIKCQPWSSMIPHEHSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRY
EVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPD
KGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECI
QGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDGS
ESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSM
WDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISR
CEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTRTNIGWMVSLRYRNKHICGGS
LIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKCKQVLNVSQLVYGPEG
SDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLR
VAHLYIMGNEKCSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKM
RMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKIILTYKVPQS. -
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
HEPATOCYTE GROWTH FACTOR HUMAN, Protein has a total Mw of 78kDa.
What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
Insect cells.
What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
HEPATOCYTE GROWTH FACTOR HUMAN, Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
The activity was assayed for scattering activity in the MDCK cell assay. The ED50 for this effect is typically at 2.0-5.0 ng/ml.
What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
QRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCK
AFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYENKDYIRNCIIGKGRSYKGT
VSITKSGIKCQPWSSMIPHEHSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRY
EVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPD
KGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECI
QGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDGS
ESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSM
WDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISR
CEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTRTNIGWMVSLRYRNKHICGGS
LIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKCKQVLNVSQLVYGPEG
SDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLR
VAHLYIMGNEKCSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKM
RMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKIILTYKVPQS.What applications can
HEPATOCYTE GROWTH FACTOR HUMAN, Protein be used in?
HEPATOCYTE GROWTH FACTOR HUMAN, Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR 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.
- View Data Sheet
Name :
IFN tau OvineDescription:
IFN-Tau Ovine Recombinant
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
Product # :
CYT-377Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IFN-Tau Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19914.7 Dalton.The IFN-Tau is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by both:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.More Info
-
Introduction
IFN-tau is also known as TP-1 (trophoblast protein-1) is a new class of type I IFN that is secreted by the trophoblast and is the signal for maternal recognition of pregnancy in sheep. IFN- tau has potent immunosuppressive and antiviral activities similar to other type I IFN but is less cytotoxic than IFN-alpha and IFN-beta. The current investigation concerns the effect of recombinant ovine IFN- tau (rOIFN- tau) on the modulation of MHC class I and II expression on cloned mouse cerebrovascular endothelial (CVE) cells.
IFN-tau induced tyrosine phosphorylation of Stat1 and upregulated the expression of MHC class I on CVE. One proposed action by which type I IFN reduces the relapse rate in MS is via interference with IFN-?-induced MHC class II expression. IFN- tau was shown to downregulate IFN-?-induced MHC class II expression on CVE and, hence, may be of potential therapeutic value in downregulating inflammation in the central nervous system (CNS). IFN- tau did not upregulate the expression of MHC class II on CVE. IFN- tau also inhibited the replication of Theiler's virus in CVE. -
Synonyms
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IFN-Tau although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Tau 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 IFN Tau in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.
-
Background
What is the molecular weight/Mw of IFN TAU OVINE Protein?
IFN TAU OVINE Protein has a total Mw of 19.9kDa.
What is the source or expression system of IFN TAU OVINE Protein?
Escherichia Coli.
What is the Purity of IFN TAU OVINE Protein?
IFN TAU OVINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN TAU OVINE Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.
What is the amino acid sequence of IFN TAU OVINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.
What applications can IFN TAU OVINE Protein be used in?
IFN TAU OVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN TAU OVINE Protein?
The endotoxin level is minimal, IFN TAU OVINE 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.
- View Data Sheet
Name :
PEX19 HumanDescription:
Peroxisomal Biogenesis Factor 19 Human Recombinant
Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.
Product # :
PRO-925Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PEX19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 34.6 kDa.The PEX19 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PEX19 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
PEX19 is vital for peroxisome biogenesis in Saccharomyces cerevisiae. PEX19 is limited to the outer surface of peroxisomes in liver cells and is has a part in the early stage of peroxisome membrane assembly, prior to the import of matrix protein.
-
Synonyms
Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.
-
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 MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQC
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 :
CNTF Rat, HisDescription:
Ciliary Neurotrophic Factor Rat Recombinant, His Tag
Ciliary neurotrophic factor, CNTF, Cntf.
Product # :
CYT-926Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CNTF Rat Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-200a.a) and having a molecular mass of 25.2kDa.CNTF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNTF protein solution (0.5mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
Ciliary neurotrophic factor, CNTF, Cntf.
-
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 MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
-
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 25.2kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
The biological functionality of CNTF Protein will be determined in the future.
What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF 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.
- View Data Sheet
Name :
EIF2B1 HumanDescription:
Eukaryotic Translation Initiation Factor 2B Subunit 1 Alpha Human Recombinant
Translation initiation factor eIF-2B subunit alpha, eIF-2B GDP-GTP exchange factor subunit alpha, EIF2B1, EIF2BA, EIF2B.
Product # :
PRO-209Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EIF2B1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (1-305 a.a.) and having a molecular mass of 35.8kDa.EIF2B1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF2B1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
EIF2B1 is one of five subunits of eukaryotic translation initiation factor 2B (EIF2B), which is a GTP exchange factor for eukaryotic initiation factor 2 and an essential regulator for protein synthesis. Phosphorylation of eIF2 inhibits GEF activity of EIF2B, an inhibition which requires the eIF2B1 subunit. Defects in eIF2B1 are a cause of leukoencephalopathy with vanishing white matter (VWM), a brain disease which is characterized by head trauma and motor deterioration.
-
Synonyms
Translation initiation factor eIF-2B subunit alpha, eIF-2B GDP-GTP exchange factor subunit alpha, EIF2B1, EIF2BA, EIF2B.
-
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 MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT SAIETLCGVD SSVAVSSGGE LFLRFISLAS LEYSDYSKCK KIMIERGELF LRRISLSRNK IADLCHTFIK DGATILTHAY SRVVLRVLEA AVAAKKRFSV YVTESQPDLS GKKMAKALCH LNVPVTVVLD AAVGYIMEKA DLVIVGAEGV VENGGIINKI GTNQMAVCAK AQNKPFYVVA ESFKFVRLFP LNQQDVPDKF KYKADTLKVA QTGQDLKEEH PWVDYTAPSL ITLLFTDLGV LTPSAVSDEL IKLYL.
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 :
FGF 2 HumanDescription:
Fibroblast Growth Factor-Basic Human Recombinant
Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.
Product # :
CYT-218Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.2kDa.The FGF-b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris-HCl, pH7.4 and 1M NaCl.
Purity
Greater than 98.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.
More Info
-
Introduction
Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The HPR -binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
-
Synonyms
Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Fibroblast Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-b 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 Fibroblast Growth Factor Basic in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.
-
Background
FGF 2 HUMAN: Insights into Fibroblast Growth Factor-2
Basic Fibroblast Growth Factor or FGF 2 HUMAN is a protein with crucial roles in cell growth, tissue repair, and embryonic development. This is part of the larger fibroblast growth factor family and is vital for various biological processes, including the modulation of cell survival activities.
Production and Properties
Produced in E. coli, FGF 2 is a non-glycosylated polypeptide chain possessing 154 amino acids with a molecular weight of about 17.2 kDa. It is purified through advanced chromatographic techniques, ensuring high purity and activity for laboratory use.
Physical Characteristics and Preparation
The physical form of FGF 2 HUMAN is a sterile, white lyophilized powder. For experimental use, it is reconstituted with sterile water to at least 100µg/ml. This reconstitution is crucial for maintaining the integrity and effectiveness of the protein in various research applications.
Storage and Handling
To maintain stability, lyophilized FGF 2 should be stored at -18°C and used within three weeks if kept at room temperature. Once reconstituted, it should be kept at 4°C and used within 2-7 days or stored at -18°C for longer-term storage.
Proper handling and avoiding repeated freeze-thaw cycles are essential to preserve the protein's functionality.
Purity and Biological Activity
FGF 2 is characterized by a purity greater than 98%, verified by SDS-PAGE analysis. Its biological activity is primarily defined by its efficacy in promoting the proliferation of specific cell lines, with an effective dose (ED50) typically below 0.1 ng/ml.
Research Applications and Impact
In the research context, FGF 2 is used extensively to study its effects on cell migration, proliferation, and angiogenesis. Moreover, its role in disease models, particularly in cancer and tissue repair studies, makes it a valuable resource for developing new therapeutic approaches.
Usage Guidelines
FGF 2 HUMAN is strictly for laboratory research use and is not suitable for drug development, food production, or cosmetic applications. Researchers are advised to comply with safety and handling guidelines to ensure that experiments are conducted under optimal conditions.
The Broad Impact on Development and Disease
FGF-2 is known for its multifunctional role across numerous biological processes such as tissue repair, embryonic development, angiogenesis, and even tumorigenesis.
This growth factor, existing in various synonymous forms such as Basic FGF, FGF-b, and HBGF-2, is essential in cellular processes that underpin both health and disease.
Furthermore, FGF-2's ability to bind to cellular receptors triggers a cascade of signaling pathways, including PI3K/Akt, MAPK/ERK, and PLCγ, which in turn influence cell growth, migration, and survival.
These pathways are pivotal in mediating the factor's diverse effects on cell behavior, contributing to its critical roles in wound healing, angiogenesis, and tissue remodeling.
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.2kDa.
What is the source or expression system of FGF 2 Protein?
Escherichia Coli.
What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.
What is the amino acid sequence of FGF 2 Protein?
AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.
What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 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.
- View Data Sheet
Name :
EREG Human, HEKDescription:
Epiregulin Human Recombinant, HEK
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
Product # :
CYT-1206Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
EREG protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
More Info
-
Introduction
"Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."
-
Synonyms
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
-
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
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
-
Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 32.6kDa.
What is the source or expression system of EREG Protein?
HEK293 cells.
What is the Purity of EREG Protein?
EREG Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
What is the amino acid sequence of EREG Protein?
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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.
- View Data Sheet
Name :
PVALB HumanDescription:
Parvalbumin Human Recombinant
Parvalbumin alpha, PVALB, D22S749, MGC116759.
Product # :
PRO-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PVALB Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-110 a.a.) and having a molecular mass of 14.6kDa. The PVALB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PVALB solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Parvalbumin alpha (PVALB) is a member of a larger group of EF hand proteins. PVALB is a high affinity calcium ion-binding protein which is structurally and functionally similar to calmodulin and troponin C. Parvalbumin is expressed in a specific population of GABAergic interneurones which are believed to have a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus.
-
Synonyms
Parvalbumin alpha, PVALB, D22S749, MGC116759.
-
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 MGSHMSMTDL LNAEDIKKAV GAFSATDSFD HKKFFQMVGLKKKSADDVKK VFHMLDKDKS GFIEEDELGF ILKGFSPDAR DLSAKETKML MAAGDKDGDG KIGVDEFSTL VAES.
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 :
Leptin Human, HisDescription:
Leptin Human Recombinant, His Tag
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-287Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Leptin is a protein hormone with important effects in regulating body weight, metabolism and reproductive function. The protein is approximately~16 kDa in mass and encoded by the obese (ob)gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus known to be important in regulating body weight, as well as in T lymphocytes and vascular endothelial cells.
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.Please avoid freeze-thaw cycles.
-
Solubility
The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.
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 :
SPA-CysDescription:
Staphylococcal Protein-A Cys Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1922Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
SPA-Cys Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain with a Cys on C-terminus. SPA-Cys is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 297 amino acids and having a molecular mass of 33.5kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by: (a) Analysis by HPLC.(b) Analysis by SDS-PAGE.
More Info
-
Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
-
Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDC
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 :
CNTF Human, His ActiveDescription:
Ciliary Neurotrophic Factor Human Recombinant, His Tag Active
Ciliary neurotrophic factor, CNTF, HCNTF.
Product # :
CYT-909Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CNTF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200 a.a) and having a molecular mass of 25kDa. CNTF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNTF protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.5), 1 mM DTT,30% Glycerol and 0.2M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.More Info
-
Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
Ciliary neurotrophic factor, CNTF, HCNTF.
-
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 MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
-
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 25kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.
What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF 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.