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1000 results found for “Stem cell”
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Name :
PSPN MouseDescription:
Persephin Mouse Recombinant
Persephin, PSPN.
Product # :
CYT-802Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.Citations
More Info
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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
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Synonyms
Persephin, PSPN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PSPN in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
STAMBPL1 HumanDescription:
STAM Binding Protein Like 1 Human Recombinant
ALMalpha, AMSH-FP, AMSH-LP, bA399O19.2, AMSH-like protease, STAM Binding Protein Like 1, STAMBPL1, AMSHLP, KIAA1373.
Product # :
PRO-1354Price :
Quantity :
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Shipped with Ice Packs
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Description
STAMBPL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 458 amino acids (1-436) and having a molecular mass of 52 kDa. STAMBPL1 is fused to a 22 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The STAMBPL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
STAM Binding Protein Like 1 (STAMBPL1) is a zinc metalloprotease which specifically cleaves 'Lys-63'-linked polyubiquitin chains, however, it doesn’t cleave 'Lys-48'-linked polyubiquitin chains. STAMBPL1 binds 2 zinc ions per subunit. The JAMM motif is vital for the protease activity. STAMBPL1 is a member of the peptidase M67C family. STAMBPL1 contains 1 MPN (JAB/Mov34) domain.
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Synonyms
ALMalpha, AMSH-FP, AMSH-LP, bA399O19.2, AMSH-like protease, STAM Binding Protein Like 1, STAMBPL1, AMSHLP, KIAA1373.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSQ SHMDQPFTVN SLKKLAAMPD HTDVSLSPEE RVRALSKLGC NITISEDITP RRYFRSGVEM ERMASVYLEE GNLENAFVLY NKFITLFVEK LPNHRDYQQC AVPEKQDIMK KLKEIAFPRT DELKNDLLKK YNVEYQEYLQ SKNKYKAEIL KKLEHQRLIE AERKRIAQMR QQQLESEQFL FFEDQLKKQE LARGQMRSQQ TSGLSEQIDG SALSCFSTHQ NNSLLNVFAD QPNKSDATNY ASHSPPVNRA LTPAATLSAV QNLVVEGLRC VVLPEDLCHK FLQLAESNTV RGIETCGILC GKLTHNEFTI THVIVPKQSA GPDYCDMENV EELFNVQDQH DLLTLGWIHT HPTQTAFLSS VDLHTHCSYQ LMLPEAIAIV CSPKHKDTGI FRLTNAGMLE VSACKKKGFH PHTKEPRLFS ICKHVLVKDI KIIVLDLR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HAVCR1 HumanDescription:
Hepatitis A Virus Cellular Receptor 1 Human Recombinant
Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.
Product # :
HAV-222Price :
Quantity :
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Shipped with Ice Packs
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Description
HAVCR1 Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (21-295aa) and having a molecular mass of 31.9kDa.HAVCR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HAVCR1 solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.
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Synonyms
Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSVKVGGE AGPSVTLPCH YSGAVTSMCW NRGSCSLFTC QNGIVWTNGT HVTYRKDTRY KLLGDLSRRD VSLTIENTAV SDSGVYCCRV EHRGWFNDMK ITVSLEIVPP KVTTTPIVTT VPTVTTVRTS TTVPTTTTVP MTTVPTTTVP TTMSIPTTTT VLTTMTVSTT TSVPTTTSIP TTTSVPVTTT VSTFVPPMPL PRQNHEPVAT SPSSPQPAET HPTTLQGAIR REPTSSPLYS YTTDGNDTVT ESSDGLWNNN QTQLFLEHSL LTANTTKG
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
sCD40L MouseDescription:
Soluble CD-40 Ligand/TRAP Mouse Recombinant
CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L.
Product # :
CYT-472Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
sCD40 Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 149 amino acids and having a molecular mass of 16409 Dalton. The sCD40 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile concentrated solution (1mg/ml) with 10mM Sodium Phosphate pH=7.5.
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 its ability to induce MIP-1 alpha & TNF-alpha from mouse splenocytes was found to be 0.1µg/ml corresponding to a Specific Activity of 10,000IU/mg.
Citations
More Info
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Introduction
CD40L or CD154 is a membrane glycoprotein and differentiation antigen expressed on the surface of T-cells. The CD40 ligand stimulates B-cell proliferation and secretion of all immunoglobulin isotypes in the presence of cytokines . CD40 ligand has been shown to induce cytokine production and tumoricidal activity in peripheral blood monocytes. It also costimulates proliferation of activated T-cells and this is accompanied by the production of IFN-gamma , TNF-alpha , and IL2 .
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Synonyms
CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized sCD40 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD154 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized sCD40 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Gln-Arg-Gly-Asp.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL4 Rhesus MacaqueDescription:
Interleukin-4 Rhesus Macaque Recombinant
Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.
Product # :
CYT-172Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL-4 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.The IL4 Rhesus Macaque is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% 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 TF1 cells is less than 0.2ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.Citations
More Info
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Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
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Synonyms
Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleikin-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HNCHIALREI IETLNSLTEQ KTLCTKLTIT DILAASKNTT EKETFCRAAT VLRQFYSHHE KDTRCLGATA QQFHRHKQLI RFLKRLDRNL WGLAGLNSCP VKEANQSTLE DFLERLKTIM REKYSKCSS.
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Background
What is the molecular weight/Mw of IL 4 RHESUS MACAQUE Protein?
IL 4 RHESUS MACAQUE Protein has a total Mw of 14.9kDa.
What is the source or expression system of IL 4 RHESUS MACAQUE Protein?
Escherichia Coli.
What is the Purity of IL 4 RHESUS MACAQUE Protein?
IL 4 RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IL 4 RHESUS MACAQUE Protein?
The ED50 as determined by the dose-dependent stimulation of TF1 cells is less than 0.2ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.
What is the amino acid sequence of IL 4 RHESUS MACAQUE Protein?
HNCHIALREI IETLNSLTEQ KTLCTKLTIT DILAASKNTT EKETFCRAAT VLRQFYSHHE KDTRCLGATA QQFHRHKQLI RFLKRLDRNL WGLAGLNSCP VKEANQSTLE DFLERLKTIM REKYSKCSS.
What applications can IL 4 RHESUS MACAQUE Protein be used in?
IL 4 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL 4 RHESUS MACAQUE Protein?
The endotoxin level is minimal, IL 4 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL 4 RHESUS MACAQUE 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 IL 4 RHESUS MACAQUE?
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.
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Name :
SHH RatDescription:
Sonic HedgeHog Rat Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Product # :
CYT-1099Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Sonic HedgeHog Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.9kDa. SHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SHH is lyophilized from a sterile (0.2 µm) filtered solution containing 10 mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog helps in guiding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is necessary for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
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Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SHH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MIIGPGRGFG KRQHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKARI HCSVKAENSV AAKSDG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ADRM1 HumanDescription:
Adhesion Regulating Molecule 1 Human Recombinant
Proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, Gp110, Adhesion-regulating molecule 1, ARM-1, Proteasome regulatory particle non-ATPase 13, hRpn13, Rpn13 homolog, ADRM1, ARM1, Rpn13.
Product # :
PRO-1079Price :
Quantity :
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Shipped with Ice Packs
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Description
ADRM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 431 amino acids (1-407 a.a) and having a molecular mass of 44.7kDa.ADRM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ADRM1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Proteasomal ubiquitin receptor ADRM1 (ADRM1) functions as a proteasomal ubiquitin receptor. ADRM1 is an integral plasma membrane protein which promotes cell adhesion. ADRM1 is assumed to undergo O-linked glycosylation. ADRM1 employs the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.
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Synonyms
Proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, Gp110, Adhesion-regulating molecule 1, ARM-1, Proteasome regulatory particle non-ATPase 13, hRpn13, Rpn13 homolog, ADRM1, ARM1, Rpn13.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTTSGA LFPSLVPGSR GASNKYLVEF RAGKMSLKGT TVTPDKRKGL VYIQQTDDSL IHFCWKDRTS GNVEDDLIIF PDDCEFKRVP QCPSGRVYVL KFKAGSKRLF FWMQEPKTDQ DEEHCRKVNE YLNNPPMPGA LGASGSSGHE LSALGGEGGL QSLLGNMSHS QLMQLIGPAG LGGLGGLGAL TGPGLASLLG SSGPPGSSSS SSSRSQSAAV TPSSTTSSTR ATPAPSAPAA ASATSPSPAP SSGNGASTAA SPTQPIQLSD LQSILATMNV PAGPAGGQQV DLASVLTPEI MAPILANADV QERLLPYLPS GESLPQTADE IQNTLTSPQF QQALGMFSAA LASGQLGPLM CQFGLPAEAV EAANKGDVEA FAKAMQNNAK PEQKEGDTKD KKDEEEDMSL D.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DIRAS1 HumanDescription:
DIRAS family, GTP-binding RAS-like 1 Human Recombinant
GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.
Product # :
PRO-256Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DIRAS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 215 amino acids (1-195a.a.) and having a molecular mass of 24.1 kDa. DIRAS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
DIRAS1 Human solution (1mg/ml) containing 20mM Tris-HCl buffer(pH 8.0) containing 20% glycerol, 1mM DTT, 0.1M NaCl and 1mM EDTA.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
DIRAS1 is a member of a distinct branch of the functionally diverse Ras superfamily of monomeric GTPases. DIRAS1 demonstrates low GTPase activity and exists mainly in the GTP-bound form. Ras proteins operate as binary molecular switches that control intracellular signaling networks. Ras-regulated signal pathways regulate such processes as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. Ras and ras-related proteins are frequently deregulated in cancers, leading to increased invasion and metastasis, and decreased apoptosis.
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Synonyms
GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPEQSNDYRV VVFGAGGVGK SSLVLRFVKG TFRDTYIPTI EDTYRQVISC DKSVCTLQIT DTTGSHQFPA MQRLSISKGH AFILVFSVTS KQSLEELGPI YKLIVQIKGS VEDIPVMLVG KCDETQREV DTREAQAVAQ EWKCAFMETS AKMNYNVKEL FQELLTLETR RNMSLNIDGK RSGKQKRTDR KGKC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LGALS3 HumanDescription:
Galectin-3 Human Recombinant
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
Product # :
CYT-606Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids and having a molecular mass of 26.2kDa. The LGALS3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-3 protein was lyophilized from a sterile 0.2 micron filtered aqueous solution containing 10 mM sodium phosphate and 50mM sodium chloride, pH 7.5.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
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Synonyms
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Galectin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized LGALS3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI.
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Background
What is the molecular weight/Mw of LGALS3 HUMAN Protein?
LGALS3 HUMAN Protein has a total Mw of 26.2kDa.
What is the source or expression system of LGALS3 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS3 HUMAN Protein?
LGALS3 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 HUMAN Protein?
The biological functionality of LGALS3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS3 HUMAN Protein?
MADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI.
What applications can LGALS3 HUMAN Protein be used in?
LGALS3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS3 HUMAN Protein?
The endotoxin level is minimal, LGALS3 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 :
TCF4 Human, sf9Description:
Transcription Factor 4 Human Recombinant, sf9
Transcription Factor 4, Class B Basic Helix-Loop-Helix Protein 19, Immunoglobulin Transcription Factor 2, SL3-3 Enhancer Factor 2, BHLHb19, ITF-2, SEF-2, TCF-4, ITF2, SEF2, SEF2-1A, SEF2-1B, SEF2-1D, SEF2-1, FECD3, E2-2, PTHS.
Product # :
PRO-2354Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TCF4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 513 amino acids (1-507a.a.) and having a molecular mass of 54.9kDa (Molecular size on SDS-PAGE will appear at approximately 35-100kDa). TCF4 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TCF4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Transcription Factor 4 (TCF4) acts as a transcription factor and takes part in the initiation of neuronal differentiation. TCF4 recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a motif primary identified in immunoglobulin enhancers. TCF4 is mainly expressed in pre-B-cells, even though it is present in other tissues as well.
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Synonyms
Transcription Factor 4, Class B Basic Helix-Loop-Helix Protein 19, Immunoglobulin Transcription Factor 2, SL3-3 Enhancer Factor 2, BHLHb19, ITF-2, SEF-2, TCF-4, ITF2, SEF2, SEF2-1A, SEF2-1B, SEF2-1D, SEF2-1, FECD3, E2-2, PTHS.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MKFKQCRCSD TGLCCLDHEG KAEVYAPSAS TADYNRDSPG YPSSKPATST FPSSFFMQDG HHSSDPWSSS SGMNQPGYAG MLGNSSHIPQ SSSYCSLHPH ERLSYPSHSS ADINSSLPPM STFHRSGTNH YSTSSCTPPA NGTDSIMANR GSGAAGSSQT GDALGKALAS IYSPDHTNNS FSSNPSTPVG SPPSLSAGTA VWSRNGGQAS SSPNYEGPLH SLQSRIEDRL ERLDDAIHVL RNHAVGPSTA MPGGHGDMHG IIGPSHNGAM GGLGSGYGTG LLSANRHSLM VGTHREDGVA LRGSHSLLPN QVPVPQLPVQ SATSPDLNPP QDPYRGMPPG LQGQSVSSGS SEIKSDDEGD ENLQDTKSSE DKKLDDDKKD IKSITSNNDD EDLTPEQKAE REKERRMANN ARERLRVRDI NEAFKELGRM VQLHLKSDKP QTKLLILHQA VAVILSLEQQ VRERNLNPKA ACLKRREEEK VSSEPPPLSL AGPHPGMGDA SNHMGQMHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MIA HumanDescription:
Melanoma Inhibitory Activity Human Recombinant
Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.
Product # :
CYT-310Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Melanoma Inhibitory Activity Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain consisting of 108 amino having a total molecular mass of 12237 Dalton.The MIA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM Potassium-phosphate pH=7 and 150mM potassium chloride.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity is calculated by the inhibiting effect on the invasion of Mel In Tumor cells and found active in Mel In assay.Citations
More Info
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Introduction
The Melanoma Inhibitory protein (MIA) was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain.
MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas. -
Synonyms
Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIA should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Melanoma Inhibitory Activity in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Agrees with the sequence of native MIA human with an addition N-terminal Methionine residue.
MGPMPKLADRKLCADQECSSHPISMAVALQDYMAPDCRFLTIHRGQVV
YVFSLKGRGRFLWGGSVQGDYYGDLAARLGYFPSSIVREDQTLKVDVKT
DKWDFYCQ. -
Protein content
UV spectroscopy at 280 nm using the absorption coefficient of 19300 M-1cm-1.
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 :
MAD2L1BP HumanDescription:
MAD2L1 Binding Protein Human Recombinant
MAD2L1-binding protein, Caught by MAD2 protein, MAD2L1BP, CMT2, KIAA0110, RP1-261G23.6.
Product # :
PRO-1052Price :
Quantity :
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Shipped with Ice Packs
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Description
MAD2L1BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-274 a.a) and having a molecular mass of 33.6kDa (Molecular weight on SDS-PAGE will appear higher).MAD2L1BP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAD2L1BP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
MAD2L1-binding protein (MAD2L1BP) is a member of the MAD2L1BP family.MAD2L1BP is a binding protein of the MAD2 mitotic arrest deficient-like 1 (MAD2/MAD2L1). MAD2 is a fundamental factor of the spindle checkpoint which delays the onset of anaphase until all the kinetochores are connected to the spindle. The MAD2L1BP protein acts to curb the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 once it dissociated from the MAD2L1-CDC20 complex. For the duration of the cell cycle, MAD2L1BP levels increase and then remain constant until late mitosis after which they drop.
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Synonyms
MAD2L1-binding protein, Caught by MAD2 protein, MAD2L1BP, CMT2, KIAA0110, RP1-261G23.6.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAPEA EVLSSAAVPD LEWYEKSEET HASQIELLET SSTQEPLNAS EAFCPRDCMV PVVFPGPVSQ EGCCQFTCEL LKHIMYQRQQ LPLPYEQLKH FYRKPSPQAE EMLKKKPRAT TEVSSRKCQQ ALAELESVLS HLEDFFARTL VPRVLILLGG
NALSPKEFYE LDLSLLAPYS VDQSLSTAAC LRRLFRAIFM ADAFSELQAP PLMGTVVMAQ GHRNCGEDWF RPKLNYRVPS RGHKLTVTLS CGRPSIRTTA WEDYIWFQAP VTFKGFRE.
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 :
OXSR1 HumanDescription:
Oxidative Stress Responsive 1 Human Recombinant
Serine/threonine-protein kinase OSR1, Oxidative stress-responsive 1 protein, KIAA1101, OSR1, OXSR1, Oxidative Stress Responsive 1.
Product # :
PRO-2104Price :
Quantity :
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Shipped with Ice Packs
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Description
OXSR1 Human Recombinant produced in E. coli is a single polypeptide chain containing 550 amino acids (1-527) and having a molecular mass of 60.4kDa.OXSR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OXSR1 solution (0.5mg/1ml) contains Phosphate Buffered Saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Oxidative Stress Responsive 1, also known as OXSR1 belongs to the neuronal calcium sensor gene family. OXSR1 encodes calcium-binding proteins which expressed mainly in neurons and regulates G protein-coupled receptor phosphorylation in a calcium-dependent way. OXSR1 regulates downstream kinases in response to environmental stress and functions in regulating the actin cytoskeleton.
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Synonyms
Serine/threonine-protein kinase OSR1, Oxidative stress-responsive 1 protein, KIAA1101, OSR1, OXSR1, Oxidative Stress Responsive 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEDSSA LPWSINRDDY ELQEVIGSGA TAVVQAAYCA PKKEKVAIKR INLEKCQTSM DELLKEIQAM SQCHHPNIVS YYTSFVVKDE LWLVMKLLSG GSVLDIIKHI VAKGEHKSGV LDESTIATIL REVLEGLEYL HKNGQIHRDV KAGNILLGED GSVQIADFGV SAFLATGGDI TRNKVRKTFV GTPCWMAPEV MEQVRGYDFK ADIWSFGITA IELATGAAPY HKYPPMKVLM LTLQNDPPSL ETGVQDKEML KKYGKSFRKM ISLCLQKDPE KRPTAAELLR HKFFQKAKNK EFLQEKTLQR APTISERAKK VRRVPGSSGR LHKTEDGGWE WSDDEFDEES EEGKAAISQL RSPRVKESIS NSELFPTTDP VGTLLQVPEQ ISAHLPQPAG QIATQPTQVS LPPTAEPAKT AQALSSGSGS QETKIPISLV LRLRNSKKEL NDIRFEFTPG RDTAEGVSQE LISAGLVDGR DLVIVAANLQ KIVEEPQSNR SVTFKLASGV EGSDIPDDGK LIGFAQLSIS.
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 :
TGIF2LX HumanDescription:
TGFB-Induced Factor Homeobox 2-Like, X-Linked Human Recombinant
Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked.
Product # :
PRO-1902Price :
Quantity :
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Shipped with Ice Packs
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Description
TGIF2LX Human Recombinant produced in E. coli is. a single polypeptide chain containing 264 amino acids (1-241) and having a molecular mass of 29.1kDa.TGIF2LX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TGIF2LX solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TGFB-Induced Factor Homeobox 2-Like, X-Linked (TGIF2LX) belongs to the TALE/TGIF homeobox family of transcription factors and takes part in spermatogenesis. A homolog of TGIF2LX is located in the male specific region of chromosome Y, in a block of sequence which is the outcome of a large X-to-Y transposition.
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Synonyms
Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein,
TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked. -
Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEAAADG PAETQSPVEK DSPAKTQSPA QDTSIMSRNN ADTGRVLALP EHKKKRKGNL PAESVKILRD WMYKHRFKAY PSEEEKQMLS EKTNLSLLQI SNWFINARRR ILPDMLQQRR NDPIIGHKTG KDAHATHLQS TEASVPAKSG PSGPDNVQSL PLWPLPKGQM SREKQPDPES APSQKLTGIA QPKKKVKVSV TSPSSPELVS PEEHADFSSF LLLVDAAVQR AAELELEKKQ EPNP.
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 :
CCL7 HumanDescription:
Monocyte Chemotactic Protein-3 Human Recombinant (CCL7)
Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.
Product # :
CHM-317Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Monocyte Chemotactic Protein-3 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 76 amino acids and having a molecular mass of 9011 Dalton. The MCP-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by the ability of MCP-3 to chemoattract human peripheral blood at 8 - 80ng/ml corresponding to a Specific Activity of 12,500-125,000IU/mg.Citations
More Info
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Introduction
Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3 (MCP3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature protein, it is classified among the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, in a large cluster containing many other CC chemokines and is most closely related to CCL2(previously called MCP1).
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Synonyms
Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MCP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL7 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Monocyte Chemotactic Protein-3in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Pro-Val-Gly-Ile.
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Background
What is the molecular weight/Mw of CCL7 HUMAN Protein?
CCL7 HUMAN Protein has a total Mw of 9.01kDa.
What is the source or expression system of CCL7 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL7 HUMAN Protein?
CCL7 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL7 HUMAN Protein?
The specific activity as determined by the ability of MCP-3 to chemoattract human peripheral blood at 8 - 80ng/ml corresponding to a Specific Activity of 12,500-125,000IU/mg.
What is the amino acid sequence of CCL7 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Pro-Val-Gly-Ile.
What applications can CCL7 HUMAN Protein be used in?
CCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL7 HUMAN Protein?
The endotoxin level is minimal, CCL7 HUMAN Protein was purified using conventional chromatography techniques.Who supplies recombinant CCL7 HUMAN 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 CCL7 HUMAN?
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.
- View Data Sheet
Name :
EPHA2 Human, sf9Description:
EPH Receptor A2 Human Recombinant, sf9
EPHA2, ARCC2, CTPA, CTPP1, CTRCT6, ECK, EPHA2, sf9, EPH Receptor A2, sf9, Ephrin type-A receptor 2.
Product # :
PRO-2332Price :
Quantity :
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Shipped with Ice Packs
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Description
EPHA2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 520 amino acids (27-537) and having a molecular mass of 57.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EPHA2 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPHA2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
EPH Receptor A2 (EPHA2) is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. EPHA2 is a protein which binds ephrin-A ligands. EPH and EPH-related receptors are associated with mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily normally have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. EPHA2 gene mutations are the cause of certain genetically-related cataract disorders.
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Synonyms
EPHA2, ARCC2, CTPA, CTPP1, CTRCT6, ECK, EPHA2, sf9, EPH Receptor A2, sf9, Ephrin type-A receptor 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPKEVVLLD FAAAGGELGW LTHPYGKGWD LMQNIMNDMP IYMYSVCNVM SGDQDNWLRT NWVYRGEAER IFIELKFTVR DCNSFPGGAS SCKETFNLYY AESDLDYGTN FQKRLFTKID TIAPDEITVS SDFEARHVKL NVEERSVGPL TRKGFYLAFQ DIGACVALLS VRVYYKKCPE LLQGLAHFPE TIAGSDAPSL ATVAGTCVDH AVVPPGGEEP RMHCAVDGEW LVPIGQCLCQ AGYEKVEDAC QACSPGFFKF EASESPCLEC PEHTLPSPEG ATSCECEEGF FRAPQDPASM PCTRPPSAPH YLTAVGMGAK VELRWTPPQD SGGREDIVYS VTCEQCWPES GECGPCEASV RYSEPPHGLT RTSVTVSDLE PHMNYTFTVE ARNGVSGLVT SRSFRTASVS INQTEPPKVR LEGRSTTSLS VSWSIPPPQQ SRVWKYEVTY RKKGDSNSYN VRRTEGFSVT LDDLAPDTTY LVQVQALTQE GQGAGSKVHE FQTLSPEGSG NLAVHHHHHH.
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 :
SPON1 HumanDescription:
Recombinant Human Spondin-1
F-Spondin, VSGP
Product # :
pro-2758Price :
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Description
SPON1 Human Recombinant produced in HEK293 cells is a single, glycosylated, polypeptide chain (29-807 a.a) containing a total of 785 amino acids, having a molecular mass of 88.9 kDa. SPON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
POR protein solution (0.25mg/ml) contains Phosphate buffer saline (pH 7.4) and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SPON1 is a cell adhesion protein which take part in the regulation of protein binding activity, regulation of protein processing and regulation of amyloid precursor protein catabolic mechanism. SPON1 is found in the extracellular space and it co-localizes with collagen-containing extracellular matrix. SPON1 stimulates the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro.
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Synonyms
F-Spondin, VSGP
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
FSDETLDKVP KSEGYCSRIL RAQGTRREGY TEFSLRVEGD PDFYKPGTSY RVTLSAAPPS YFRGFTLIAL RENREGDKEE DHAGTFQIID EEETQFMSNC PVAVTESTPR RRTRIQVFWI APPAGTGCVI LKASIVQKRI IYFQDEGSLT KKLCEQDSTF DGVTDKPILD CCACGTAKYR LTFYGNWSEK THPKDYPRRA NHWSAIIGGS HSKNYVLWEY GGYASEGVKQ VAELGSPVKM EEEIRQQSDE VLTVIKAKAQ WPAWQPLNVR AAPSAEFSVD RTRHLMSFLT MMGPSPDWNV GLSAEDLCTK ECGWVQKVVQ DLIPWDAGTD SGVTYESPNK PTIPQEKIRP LTSLDHPQSP FYDPEGGSIT QVARVVIERI ARKGEQCNIV PDNVDDIVAD LAPEEKDEDD TPETCIYSNW SPWSACSSST CDKGKRMRQR MLKAQLDLSV PCPDTQDFQP CMGPGCSDED GSTCTMSEWI TWSPCSISCG MGMRSRERYV KQFPEDGSVC TLPTEETEKC TVNEECSPSS CLMTEWGEWD ECSATCGMGM KKRHRMIKMN PADGSMCKAE TSQAEKCMMP ECHTIPCLLS PWSEWSDCSV TCGKGMRTRQ RMLKSLAELG DCNEDLEQVE KCMLPECPID CELTEWSQWS ECNKSCGKGH VIRTRMIQME PQFGGAPCPE TVQRKKCRIR KCLRNPSIQK LRWREARESR RSEQLKEESE GEQFPGCRMR PWTAWSECTK LCGGGIQERY MTVKKRFKSS QFTSCKDKKE IRACNVHPC-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 :
CXCL8 Human, GSTDescription:
Interleukin-8 (1-72) (CXCL8) Human Recombinant, GST Tag
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
Product # :
CHM-047Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
IL8 GST solution contains 25mM Tris-Base/ 25mM K2CO3.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Applications
Immunoassay.
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Background
What is the source or expression system of CXCL8 HUMAN, GST Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, GST Protein?
The biological functionality of CXCL8 HUMAN, GST Protein will be determined in the future.
What is the amino acid sequence of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is composed from 72 amino acids.
What applications can CXCL8 HUMAN, GST Protein be used in?
CXCL8 HUMAN, GST Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, GST Protein?
The endotoxin level is minimal, CXCL8 HUMAN, GST Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL8 HUMAN, GST 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 CXCL8 HUMAN, GST?
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.
- View Data Sheet
Name :
CCL22 RatDescription:
Macrophage-Derived Chemokine (CCL22) Rat Recombinant
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.
Product # :
CHM-279Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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- Citations
Description
CCL22 Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.9kDa. The Rat CCL22 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10.0-100.0 ng/ml.Citations
More Info
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Introduction
MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16.
MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer. -
Synonyms
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MDC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution MDC should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized MDC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GPYGANVEDS ICCQDYIRHP LPPRFVKEFY WTSKSCRKPG VVLITIKNRD ICADPRMLWV KKILHKLA.
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Background
What is the molecular weight/Mw of CCL22 RAT Protein?
CCL22 RAT Protein has a total Mw of 7.9kDa.
What is the source or expression system of CCL22 RAT Protein?
Escherichia Coli.
What is the Purity of CCL22 RAT Protein?
CCL22 RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL22 RAT Protein?
Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10.0-100.0 ng/ml.
What is the amino acid sequence of CCL22 RAT Protein?
GPYGANVEDS ICCQDYIRHP LPPRFVKEFY WTSKSCRKPG VVLITIKNRD ICADPRMLWV KKILHKLA
What applications can CCL22 RAT Protein be used in?
CCL22 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL22 RAT Protein?
The endotoxin level is minimal, CCL22 RAT Protein was purified using conventional chromatography techniques.Who supplies recombinant CCL22 RAT 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 CCL22 RAT?
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.
- View Data Sheet
Name :
EGF HumanDescription:
Epidermal Growth Factor Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-217Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.
Citations
More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
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Background
About EGF:
In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF).
Description:
Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses.
Function:
By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers.
Mechanism:
EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.
What is the source or expression system of EGF Protein?
Escherichia Coli.
What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.
What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL1B MouseDescription:
Interleukin-1 beta Mouse Recombinant
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
CYT-273Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
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Description
Interleukin-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17500 Dalton. The IL-1b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Mouse IL-1b was lyophilized from a sterile filtered aqueous solution in 10mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity as determined by the dose-dependent proliferation of mouse D10S cells is 0.9-1.3pg/ml, corresponding to a Specific Activity of 1.1 x 106 Units/mg.Citations
More Info
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Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.
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Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1b should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MVPIRQLHYR LRDEQQKSLV LSDPYELKAL HLNGQNINQQ VIFSMSFVQGEPSNDKIPVA LGLKGKNLYL SCVMKDGTPT LQLESVDPKQ YPKKKMEKRFVFNKIEVKSK VEFESAEFPN WYISTSQAEH KPVFLGNNSG QDIIDFTMES VSS.
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Background
What is the molecular weight/Mw of IL1B MOUSE Protein?
IL1B MOUSE Protein has a total Mw of 17.5kDa.
What is the source or expression system of IL1B MOUSE Protein?
Escherichia Coli.
What is the Purity of IL1B MOUSE Protein?
IL1B MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL1B MOUSE Protein?
The activity as determined by the dose-dependent proliferation of mouse D10S cells is 0.9-1.3pg/ml, corresponding to a Specific Activity of 1.1 x 106 Units/mg.
What is the amino acid sequence of IL1B MOUSE Protein?
MVPIRQLHYR LRDEQQKSLV LSDPYELKAL HLNGQNINQQ VIFSMSFVQGEPSNDKIPVA LGLKGKNLYL SCVMKDGTPT LQLESVDPKQ YPKKKMEKRFVFNKIEVKSK VEFESAEFPN WYISTSQAEH KPVFLGNNSG QDIIDFTMES VSS.
What applications can IL1B MOUSE Protein be used in?
IL1B MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL1B MOUSE Protein?
The endotoxin level is minimal, IL1B MOUSE 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 :
STAT1 AntibodyDescription:
STAT1, Mouse Anti Human
Signal transducer and activator of transcription 1-alpha/beta, Transcription factor ISGF-3 components p91/p84, STAT1, ISGF-3, STAT91, DKFZp686B04100.
Product # :
ANT-468Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
- Citations
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
Citations
More Info
-
Introduction
STAT1 is a member of the Signal Transducers and Activators of Transcriptionfamily of transcription factors. STAT1 is involved in upregulating genes due to a signal by either type Ior type IIinterferons. In response to IFN-?stimulation, STAT1 forms homodimers or heterodimers with STAT3that bind to the GAS (Interferon-Gamma Activated Sequence) promoter element; in response to either IFN-? or IFN-?stimulation, STAT1 forms a heterodimer with STAT2that can bind the ISRE (Interferon Stimulated Response Element) promoter element. In either case, binding of the promoter element leads to an increased expression of ISG (Interferon Stimulated Genes).
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Synonyms
Signal transducer and activator of transcription 1-alpha/beta, Transcription factor ISGF-3 components p91/p84, STAT1, ISGF-3, STAT91, DKFZp686B04100.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human STAT1 mAb, clone PAT1F4A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human STAT1 protein 1-712 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and Kappa light chain.
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Clone
PAT1F4A.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:1000. Recommended starting dilution is 1:500.
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Type
Mouse Anti Human Monoclonal.
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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.
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 :
SIRT2 HumanDescription:
Sirtuin 2 Human Recombinant
Sirtuin 2, SIR2L2, SIR2-like protein 2, NAD-dependent deacetylase sirtuin-2, Silent Information Regulator 2.
Product # :
PRO-033Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
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Description
SIRT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (1-352a.a.) and having a molecular mass of 41.7kDa.SIRT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SIRT2 protein solution (0.25mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 2mM DTT, 200mM NaCl, 0.5mM EDTA and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SIRT2 belongs to the sirtuin family of proteins, homologs to the yeast Sir2 protein. Proteins of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes and take part in various processes, including transcriptional regulation, cell cycle progression, DNA-damage repair and aging. SIRT2 is a NAD-dependent deacetylase, which deacetylates the 'Lys-40' of alpha-tubulin.
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Synonyms
Sirtuin 2, SIR2L2, SIR2-like protein 2, NAD-dependent deacetylase sirtuin-2, Silent Information Regulator 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDFLRNLFSQ TLSLGSQKER LLDELTLEGV ARYMQSERCR RVICLVGAGI STSAGIPDFR SPSTGLYDNL EKYHLPYPEA IFEISYFKKH PEPFFALAKE LYPGQFKPTI CHYFMRLLKD KGLLLRCYTQ NIDTLERIAG LEQEDLVEAH GTFYTSHCVS ASCRHEYPLS WMKEKIFSEV TPKCEDCQSL VKPDIVFFGE SLPARFFSCM QSDFLKVDLL LVMGTSLQVQ PFASLISKAP LSTPRLLINK EKAGQSDPFL GMIMGLGGGM DFDSKKAYRD VAWLGECDQG CLALAELLGW KKELEDLVRR EHASIDAQSG AGVPNPSTSA SPKKSPPPAK DEARTTEREK PQ
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 :
VWA2 HumanDescription:
Von Willebrand Factor A Domain Containing 2 Human Recombinant
A domain-containing protein similar to matrilin and collagen, AMACO, Colon cancer secreted protein 2, CCSP-2.
Product # :
PRO-2752Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VWA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (341-517 a.a) and having a molecular mass of 19.3kDa.The VWA2 is expressed with an amino-terminal hexahistidine tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The VWA2 protein solution contains 20mM Tris-HCl, pH 8.0, 0.8M Urea & 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Von Willebrand Factor A Domain Containing 2 (VWA2) is an extracellular matrix protein containing vWA-like domains. VWA2 contains a signal peptide sequence, an N-terminal VWA domain connected to 2 additional tandem vWA domains by a cysteine-rich sequence and an EGF-like domain. Also, another EGF-like domain is located at the C-terminus. Expression of VWA2 is induced in stage II, III and IV colon cancers and colon adenomas and is considered a novel serum marker for the diagnosis of early-stage colon cancer.
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Synonyms
A domain-containing protein similar to matrilin and collagen, AMACO, Colon cancer secreted protein 2, CCSP-2.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.