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Name :
RPS10 HumanDescription:
Ribosomal Protein S10 Human Recombinant
DBA9, S10, 40S ribosomal protein S10, RPS10.
Product # :
PRO-1409Price :
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Shipped with Ice Packs
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Description
RPS10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 21kDa. RPS10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RPS10 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Ribosomes (the organelles that catalyze protein synthesis) consist of a small 40S subunit and a large 60S subunit. Jointly these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPS10 which is is located in the cytoplasm and a part of the S10E family of ribosomal proteins, is a ribosomal protein that is a component of the 40S subunit. Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found.
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Synonyms
DBA9, S10, 40S ribosomal protein S10, RPS10.
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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 MGSMLMPKKN RIAIYELLFK EGVMVAKKDV HMPKHPELAD KNVPNLHVMK AMQSLKSRGY VKEQFAWRHF YWYLTNEGIQ YLRDYLHLPP EIVPATLRRS RPETGRPRPK GLEGERPARL TRGEADRDTY RRSAVPPGAD KKAEAGAGSA TEFQFRGGFG RGRGQPPQ.
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 HumanDescription:
Sonic HedgeHog Human Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Product # :
CYT-676Price :
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Shipped at Room temp
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Description
Sonic HedgeHog Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 20.2kDa. The Cys at position 2 has been substituted with 2 Ile’s.
Source
Escherichia Coli.
Formulation
SHH is lyophilized from 10mM Na3PO4, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 is measured by the dose-dependent induction of alkaline phosphatase production by CCL-226 fibroblasts and is 1.47μg/ml corresponding to a specific activity of 680U/mg.
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 is a protein that is vital in guding 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 functions in 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 essential 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 water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRALDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGGCFP
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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Description:
Porcine Follicle Stimulating Hormone
Follitropin, Follicle-stimulating hormone, FSH.
Product # :
HOR-285Price :
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Description
FSH Porcine is a glycoprotein produced from pituitaries of porcine. The FSH is purified by proprietary chromatographic techniques.
Source
Porcine pituitaries.
Formulation
The FSH was lyophilized with no additives.
More Info
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Introduction
Follicle stimulating hormone (FSH) is a hormone synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproductionIn women, in the ovary FSH stimulates the growth of immature Graafian follicles to maturation. As the follicle grows it releases inhibin, which shuts off the FSH production.
In men, FSH enhances the production of androgen-binding proteinby the Sertoli cells of the testes and is critical for spermatogenesis.
In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, specifically affecting granulosa cells. With the concomitant rise in inhibin B FSH levels then decline in the late follicular phase. This seems to be critical in selecting only the most advanced follicle to proceed to ovulation. At the end of the luteal phase, there is a slight rise in FSH that seems to be of importance to start the next ovulatory cycle.
Like its partner, LH, FSH releas -
Synonyms
Follitropin, Follicle-stimulating hormone, FSH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized porcine FSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FSH-porcine 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 porcine FSH in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Specific Activity
40 Units/1mg.
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 :
AKR7A3 AntibodyDescription:
Aldo-Keto Reductase Family 7 Member A3, Mouse Anti Human
AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.
Product # :
ANT-066Price :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
AKR7A3, takes part in the detoxification of aldehydes and ketones. AKR7A3 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A3 participates in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.
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Synonyms
AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.
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Immunogen
Anti-human AKR7A3, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human AKR7A3 amino acids 1-331 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT2E11.
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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 1:1000.
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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.
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Purification Method
AKR7A3 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GHBP Human, HisDescription:
Growth Hormone Binding Protein Human Recombinant, His Tag
Growth Hormone Receptor, Growth Hormone Binding Protein, Somatotropin Receptor GH Receptor, Serum Binding Protein, GHBP, GHIP.
Product # :
CYT-921Price :
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Shipped with Ice Packs
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Description
GHBP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 254 amino acids (19-264a.a.) and having a molecular mass of 29.4kDa.GHBP is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
GHBP protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 10ng/ml and is measured by ability to inhibit GH-induced proliferation assay using Nb2-11 Rat lymphoma cells in the presence of 1.25ng/ml of human growth hormone.
More Info
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Introduction
Growth hormone receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, growth hormone performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.
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Synonyms
Growth Hormone Receptor, Growth Hormone Binding Protein, Somatotropin Receptor GH Receptor, Serum Binding Protein, GHBP, GHIP.
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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
FSGSEATAAI LSRAPWSLQS VNPGLKTNSS KEPKFTKCRS PERETFSCHW TDEVHHGTKN LGPIQLFYTR RNTQEWTQEW KECPDYVSAG ENSCYFNSSF TSIWIPYCIK LTSNGGTVDE KCFSVDEIVQ PDPPIALNWT LLNVSLTGIH ADIQVRWEAP RNADIQKGWM VLEYELQYKE
VNETKWKMMD PILTTSVPVY SLKVDKEYEV RVRSKQRNSG NYGEFSEVLY VTLPQMSQFT CEEDFYLEHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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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 :
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Shipped at Room temp
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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
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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.
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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.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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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.
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Name :
AKR1C1 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member C1 Human Recombinant, His Tag
DDH1, DDH, HAKRC, 20-alpha-HSD, DD1/DD2, HBAB, C9, DD1, H-37, MBAB, MGC8954, 2-ALPHA-HSD, AKR1C1, Aldo-keto reductase family 1 member C1, 20-alpha-hydroxysteroid dehydrogenase, Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, Indanol dehydrogenase, Dihydrodiol dehydrogenase 1/2, Chlordecone reductase homolog HAKRC, High-affinity hepatic bile acid-binding protein.
Product # :
ENZ-496Price :
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Shipped with Ice Packs
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Description
AKR1C1 Human Recombinant fused to a 20 amino acid His Tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 38.9 kDa. The AKR1C1 is fused to a 20 a.a. His Tag at n-terminal and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1C1 protein solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 500 pmol/min/ug, and is defined as the amount of enzyme that catalyze the oxidation of 1.0 pmole 1-Acenaphthenol in the presence of NADP per minute at pH 8.8 at 25°C.More Info
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Introduction
AKR1C1 transfers progesterone to its inactive state or in other words catalyzes the reaction of 20-alpha-hydroxy progesterone (20-alpha-OHP). In the liver and intestine. AKR1C1 transfers bile and monitors the intrahepatic bile acid concentration though it has a low bile-binding ability. AKR1C1 participates in myelin formation. AKR1C1 is part of the aldo/keto reductase superfamily, which has over 40 known enzymes which catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors thus display overlapping but distinct substrate specificity.
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Synonyms
DDH1, DDH, HAKRC, 20-alpha-HSD, DD1/DD2, HBAB, C9, DD1, H-37, MBAB, MGC8954, 2-ALPHA-HSD, AKR1C1, Aldo-keto reductase family 1 member C1, 20-alpha-hydroxysteroid dehydrogenase, Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, Indanol dehydrogenase, Dihydrodiol dehydrogenase 1/2, Chlordecone reductase homolog HAKRC, High-affinity hepatic bile acid-binding protein.
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Physical Appearance
Sterile Filtered clear 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 MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA VEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN RNVRYLTLDI FAGPPNYPFS DEY.
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 :
SMAD3 HumanDescription:
Mothers Against Decapentaplegic Homolog 3 Human Recombinant
MADH3, JV15-2, HSPC193, HsT17436, MGC60396, DKFZp586N0721, DKFZp686J10186, SMAD3, Mothers against decapentaplegic homolog 3, Mothers against DPP homolog 3, MAD homolog 3, Mad3, hMAD-3, SMAD family member 3, SMAD 3, hSMAD3.
Product # :
PRO-751Price :
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Shipped with Ice Packs
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Description
SMAD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 445 amino acids (1-425) and having a molecular mass of 50.2 kDa. SMAD3 is fused to a 20 amino acid His-Tag at N-Terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The SMAD3 protein solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 0.1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SMAD3 is part of the SMAD family of proteins that mediate signal transduction by the TGF-beta/activin/BMP-2/4 cytokine superfamily from receptor Ser/Thr protein kinases at the cell surface to the nucleus. SMAD3 has a role as a transcriptional modulator activated by TGF-Beta and is involved in the regulation of carcinogenesis. SMAD3 mutations are related with the pathogenesis of human osteoarthritis. SMAD3 expression take part in tumor suppression in the premature stages of gastric carcinogenesis. SMAD3 is involved in nuclear translocation of beta-catenin.
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Synonyms
MADH3, JV15-2, HSPC193, HsT17436, MGC60396, DKFZp586N0721, DKFZp686J10186, SMAD3, Mothers against decapentaplegic homolog 3, Mothers against DPP homolog 3, MAD homolog 3, Mad3, hMAD-3, SMAD family member 3, SMAD 3, hSMAD3.
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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 MSSILPFTPP IVKRLLGWKK GEQNGQEEKW CEKAVKSLVK KLKKTGQLDE LEKAITTQNV NTKCITIPRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELRAMELCE FAFNMKKDEV CVNPYHYQRV ETPVLPPVLV PRHTEIPAEF PPLDDYSHSI PENTNFPAGI EPQSNIPETP PPGYLSEDGE TSDHQMNHSM DAGSPNLSPN PMSPAHNNLD LQPVTYCEPA FWCSISYYEL NQRVGETFHA SQPSMTVDGF TDPSNSERFC LGLLSNVNRN AAVELTRRHI GRGVRLYYIG GEVFAECLSD SAIFVQSPNC NQRYGWHPAT VCKIPPGCNL KIFNNQEFAA LLAQSVNQGF EAVYQLTRMC TIRMSFVKGW GAEYRRQTVT STPCWIELHL NGPLQWLDKV LTQMGSPSIR CSSVS.
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 :
HSA Recombinant, PlantDescription:
Human Serum Albumin Recombinant, Plant
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-595Price :
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Shipped at Room temp
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Description
HSA Human Recombinant produced in Plant is a non-glycosylated, polypeptide chain containing 585 amino acids and having a molecular mass of 67 kDa. The optimum concentration for recombinant Albumin to be used in cell culture ranges between 0.5gr to 2gr per liter. The recombinant Albumin is purified by proprietary chromatographic techniques.
Source
Rice Grain.
Formulation
The Recombinant Albumin was lyophilized with sodium chloride. A 10% w/v solution when dissolved in water will contain 50mM NaCl.
Purity
Greater than 98% as determined by SDS-PAGE.
More Info
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Introduction
Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood. -
Synonyms
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Recombinant Albumin although stable at 4°C for 3 weeks, should be stored at -18°C.Please prevent freeze-thaw cycles.
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Applications
Recombinant Albumin can be used as a media culture supplement at concentrations up to 5 grams per liter. Gradual adaptation of cell lines over several passages to a concentration of 0.5gr to 2gr per liter.
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 :
IL 22 Mouse, PEGDescription:
Interleukin-22 Mouse Recombinant, Pegylated
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Product # :
CYT-701Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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Description
Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated solution at 0.65mg/ml containing 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by STAT3 phosphorylation assay in HepG cells. The activity in vitro was found to be ~ 10% compared to the non-pegylated mouse IL22.More Info
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Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10Rβ (previously known as CRF2-4), belonging to the class II cytokine recep
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Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized pegylated murine IL22 although stable at room temperature for several days, should be stored desiccated below -20°C. Upon reconstitution at 0.1mg/ml pegylated mouse IL22 and up to 2mg/ml, filter and sterilized, the protein can be stored at 4 degrees Celsius for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized pegylated mouse Interleukin -22 in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL21 Human, Sf9Description:
Interleukin-21, Sf9 Human Recombinant
Interleukin-21 isoform 1, CVID11, IL-21, Za11.
Product # :
CYT-1072Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 145 amino acids (30-162a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL21 is expressed with a 12 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL21 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-21 isoform 1 or IL21, categorized as a T helper cytokine. IL21 is part of the regulation of immune responses, haematopoiesis and cell-mediated responses. IL21 has a key role in haematopoiesis and immune responses regulation, therefore can affect lymphocyte development. Activation of T cells leads to production of the IL21. The protein has a crucial role in the viral infections persistence.
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Synonyms
Interleukin-21 isoform 1, CVID11, IL-21, Za11.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPEFMQGQD RHMIRMRQLI DIVDQLKNYV NDLVPEFLPA PEDVETNCEW SAFSCFQKAQ LKSANTGNNE RIINVSIKKL KRKPPSTNAG
RRQKHRLTCP SCDSYEKKPP KEFLERFKSL LQKMIHQHLS SRTHGSEDSH 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 :
IRF5 HumanDescription:
IFN Regulatory Factor-5 Human Recombinant
IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.
Product # :
CYT-816Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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- More Info
- SDS-PAGE
Description
IRF5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (176-240a.a) and having a molecular mass of 10.7kDa.IRF5 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IRF5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
SDS-PAGE
More Info
-
Introduction
IFN Regulatory Factor-5, also known as IRF5 belongs to the IFN regulatory factor (IRF) family, a group of transcription factors with various functions, including virus-mediated activation of IFN, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Multiple transcript variants encoding different isoforms have been found for this gene. In addition, IRF5 is implicated in the induction of IFNs IFNA and INFB and inflammatory cytokines upon virus infection. IRF5 is activated by TLR7 or TLR8 signaling.
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Synonyms
IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I
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Background
What is the molecular weight/Mw of IRF5 HUMAN Protein?
IRF5 HUMAN Protein has a total Mw of 10.7kDa.
What is the source or expression system of IRF5 HUMAN Protein?
Escherichia Coli.
What is the Purity of IRF5 HUMAN Protein?
IRF5 HUMAN Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of IRF5 HUMAN Protein?
The biological functionality of IRF5 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IRF5 HUMAN Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I
What applications can IRF5 HUMAN Protein be used in?
IRF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IRF5 HUMAN Protein?
The endotoxin level is minimal, IRF5 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 :
Lamin-A HumanDescription:
Lamin-A Human Recombinant
Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
Product # :
PRO-690Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Lamin A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids and having a molecular mass of 70 kDa. Lamin-A protein is fused to a 6xHis tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The Lamin-A Protein solution (0.9mg/ml) contains 20mM phosphate buffer pH 7.0, 500mM NaCl, 1mM DTT, 1.5mM EDTA and 20% (v/v) Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. -
Synonyms
Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRS
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 :
IL 1RA HumanDescription:
Interleukin-1 Receptor Antagonist Human Recombinant
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Product # :
CYT-203Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL1ra Human Recombinant produced in E.Coli is a non-glycosylated, N-terminal methionyl form of the human naturally-occurring polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton. The IL1ra is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized protein with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant inhibition of IL-1 stimulation of D10S cells was found to be 0.5 ng/ml corresponding to a Specific Activity of 2,000,000IU/mg.More Info
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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
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Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin 1ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1ra 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-1 ra 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
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.89 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 ra as a Reference Standard.
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 :
GH Human, HEKDescription:
Growth Hormone Human Recombinant, HEK
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-091Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Growth Hormone Human Recombinant produced in HEK cells is a non-glycosylated monomer, having a total molecular weight of 22kDa.The GH is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The GH was lyophilized from 1.13mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The activity was determined by the dose dependent stimulation of the proliferation of rat lymphoma line Nb2-11 cells (prolactin indicator cell line), the ED50 is 0.1ng/ml.
More Info
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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH 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 GH in sterile 1xPBS containing 0.1% endotoxin-free recombinant HSA.
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 :
HN1L HumanDescription:
Hematological and Neurological Expressed 1-Like Human Recombinant
C16orf34, L11, Hematological and neurological expressed 1-like protein, HN1-like protein.
Product # :
PRO-027Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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Description
HN1L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a.) and having a molecular mass of 22.5kDa.HN1L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HN1L protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Hematological and neurological expressed 1-like ( HN1L) is a member of the HN1 family.HN1L is anticipated to participate in embryo development. HN1L is expressed in a variety of tissues for example :liver, kidney, prostate, testis and uterus at different levels.
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Synonyms
C16orf34, L11, Hematological and neurological expressed 1-like protein, HN1-like protein.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMFQVPDS EGGRAGSRAM KPPGGESSNL FGSPEEATPS SRPNRMASNI FGPTEEPQNI PKRTNPPGGK GSGIFDESTP VQTRQHLNPP GGKTSDIFGS PVTATSRLAH PNKPKDHVFL CEGEEPKSDL KAARSIPAGA EPGEKGSARK AGPAKEQEPM PTVDSHEPRL GPRPRSHNKV LNPPGGKSSI SFY.
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 :
BD 1 HumanDescription:
Beta Defensin-1 Human Recombinant
Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.
Product # :
CYT-564Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- purity
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Description
Beta Defensin-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 47 amino acids and having a molecular mass of 5 kDa.The BD-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Human BD-1 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM sodium chloride.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.More Info
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Synonyms
Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Beta Defensin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 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 Beta Defensin-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.
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Background
Beta Defensin-1 Human Recombinant: Unveiling its Potential in Innate Immunity and Therapeutic Applications
Abstract:
Beta Defensin-1 (BD-1), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-1 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-1 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-1, highlighting its impact on innate immunity and its therapeutic potential.Introduction:
Innate immunity serves as the first line of defense against invading pathogens. BD-1, a key peptide within the defensin family, exhibits broad-spectrum antimicrobial activity and plays a pivotal role in host defense mechanisms. This paper provides an overview of BD-1, shedding light on its structure, function, and therapeutic potential.BD-1 Structure and Function:
BD-1 is a cationic peptide with a conserved cysteine motif that confers its antimicrobial properties. It acts by disrupting the integrity of microbial cell membranes, leading to microbial death. Additionally, BD-1 exhibits immunomodulatory effects by stimulating immune cell recruitment and cytokine production.Antimicrobial Properties and Therapeutic Applications:
BD-1 demonstrates antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Its ability to combat multidrug-resistant strains makes it an attractive candidate for the development of novel antimicrobial therapies. Furthermore, BD-1's immunomodulatory effects contribute to its potential in treating inflammatory and infectious diseases.Therapeutic Potential of BD-1 Human Recombinant:
BD-1 human recombinant holds significant promise in the field of immunotherapy. Strategies aimed at enhancing BD-1 expression or delivering exogenous BD-1 may help boost innate immune responses in patients with compromised immune systems or chronic infections. Furthermore, BD-1-based therapeutics could be developed to combat antibiotic-resistant infections and prevent biofilm formation.Challenges and Future Directions:
While BD-1 shows immense therapeutic potential, challenges must be addressed. Further research is necessary to optimize the delivery methods of BD-1 and evaluate its long-term safety and efficacy. Additionally, understanding the interplay between BD-1 and other immune factors will aid in developing combinatorial approaches for enhanced therapeutic outcomes.Conclusion:
BD-1 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-1 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize the field of immunotherapy and improve patient outcomes.What is the molecular weight/Mw of BD1 Protein?
BD1 Protein has a total Mw of 5kDa.
What is the source or expression system of BD1 Protein?
Escherichia Coli.
What is the Purity of BD1 Protein?
BD1 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BD1 Protein?
Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.
What is the amino acid sequence of BD1 Protein?
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.
What applications can BD1 Protein be used in?
BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD1 Protein?
The endotoxin level is minimal, BD1 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 :
IL 12 p40 Human BaculovirusDescription:
Interleukin-12 p40 Human Recombinant, Baculovirus
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
Product # :
CYT-134Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL 12 p40 Human Recombinant produced in Hi-5 cell using Baculovirus is a single polypeptide chain containing 315 amino acids (23-328) and having a molecular mass of 35.8kDa.IL 12 p40 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Baculovirus
Formulation
The IL 12 p40 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT, 100mM PMSF and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
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Synonyms
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPIWELKKD VYVVELDWYP DAPGEMVVLT CDTPEEDGIT WTLDQSSEVL GSGKTLTIQV KEFGDAGQYT CHKGGEVLSH SLLLLHKKED GIWSTDILKD QKEPKNKTFL RCEAKNYSGR FTCWWLTTIS TDLTFSVKSS RGSSDPQGVT CGAATLSAER VRGDNKEYEY SVECQEDSAC PAAEESLPIE VMVDAVHKLK YENYTSSFFI RDIIKPDPPK NLQLKPLKNS RQVEVSWEYP DTWSTPHSYF SLTFCVQVQG KSKREKKDRV FTDKTSATVI CRKNASISVR AQDRYYSSSW SEWASVPCSH 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.
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Name :
IL 2 MouseDescription:
Interleukin-2 Mouse Recombinant
Interleukin-2, T-cell growth factor (TCGF), Lymphokine, IL-2.
Product # :
CYT-370Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids and having a molecular mass of 17.2kDa. The IL-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution (1mg/ml) in 20mM PBS, 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-dependant stimulation of murine CTLL-2 cells is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.More Info
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Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
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Synonyms
Interleukin-2, T-cell growth factor (TCGF), Lymphokine, IL-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 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 Mouse IL-2 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
PTSSSTSSST AEAQQQQQQQ QQQQQHLEQL LMDLQELLSR MENYRNLKLP RMLTFKFYLP KQATELKDLQ CLEDELGPLR HVLDLTQSKS FQLEDAENFI SNIRVTVVKL KGSDNTFECQ FDDESATVVD FLRRWIAFCQ SIISTSPQ.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.482 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-2 as a Reference Standard.
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 :
STX4 HumanDescription:
Syntaxin-4 Human Recombinant
Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.
Product # :
PRO-1176Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
STX4 Human Recombinant produced in E. coli is a single polypeptide chain containing 300 amino acids (1-275) and having a molecular mass of 34.7 kDa.STX4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The STX4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Syntaxin 4 (STX4) is a member of the syntaxin/epimorphin family of proteins. The Syntaxin family is cellular receptors for transport vesicles which participate in exocytosis in neutrophils. Syntaxin 4 is vital for normal regulation of glucose metabolism uptake in skeletal muscle and decline in STX4 protein levels lead to reduction of whole-body hormone-stimulated glucose metabolism. STX4 is expressed in neutrophils and neutrophil-differentiated HL-60 cells. The STX4 expression in neutrophils increases with differentiation.
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Synonyms
Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.
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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 MGSHMMRDRT HELRQGDDSS DEEDKERVAL VVHPGTARLG SPDEEFFHKV RTIRQTIVKL GNKVQELEKQ QVTILATPLP EESMKQELQN LRDEIKQLGR EIRLQLKAIE PQKEEADENY NSVNTRMRKT QHGVLSQQFV ELINKCNSMQ SEYREKNVER IRRQLKITNA GMVSDEELEQ MLDSGQSEVF VSNILKDTQV TRQALNEISA RHSEIQQLER SIRELHDIFT FLATEVEMQG EMINRIEKNI LSSADYVERG QEHVKTALEN QKKARKKKVL
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 :
IL 9 HumanDescription:
Interleukin-9 Human Recombinant
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
Product # :
CYT-348Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-9 Human Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14,004 Dalton. The IL-9 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-9 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, 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 human MO7e cells is less than 0.2 ng/ml, corresponding to a Specific Activity of >5.0×106 IU/mg.More Info
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Introduction
Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
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Synonyms
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 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-9 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
MQGCPTLAGI LDINFLINKM QEDPASKCHC SANVTSCLCL GIPSDNCTRP CFSERLSQMT NTTMQTRYPL IFSRVKKSVE VLKNNKCPYF SCEQPCNQTT AGNALTFLKS LLEIFQKEKM RGMRGKI.
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 :
IL10RA HumanDescription:
Interleukin 10 Receptor Alpha Human Recombinant
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
Product # :
CYT-892Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
IL10RA Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated, polypeptide chain containing 220 amino acids (22-235 a.a.) and having a molecular mass of 25.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).IL10RA is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The IL10RA protein solution (0.2mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
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Synonyms
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
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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
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS LLTSGEVGEF CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH
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 :
IL1F10 HumanDescription:
Interleukin 1 Family, Member 10 Human Recombinant
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
Product # :
CYT-012Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
IL1F10 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 152 amino acids and having a molecular mass of 17kDa.The IL1F10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL1F10 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
As measured by its binding ability in a functional ELISA, immobilized IL1F10 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.
More Info
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Introduction
Human interleukin family 1, member 10 (IL1F10) belongs to the interleukin 1 cytokine family. IL1F10 is expressed in the fetal skin, spleen and tonsil, generally in the basal epithelia of skin and in proliferating B-cells of the tonsil. IL1F10 binds soluble IL1 receptor type 1 and may be implicated in the regulation of adapted and innate immune responses.
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Synonyms
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL1F10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F10 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 quick spin followed by reconstitution of IL1F10 in PBS to a concentration no less than 100 µg/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-Cys-Ser-Leu-Pro.
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 :
ZNF32 HumanDescription:
Zinc Finger Protein 32 Human Recombinant
KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.
Product # :
PRO-1983Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ZNF32 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273 a.a) and having a molecular mass of 33.4kDa. ZNF32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZNF32 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Zinc Finger Protein 32 (ZNF32) is a part of the krueppel C2H2-type zinc-finger protein family. ZNF32 which contains seven C2H2-type zinc fingers takes part in transcriptional regulation.
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Synonyms
KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.
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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 MGSMFGFPTA TLLDCHGRYA QNVAFFNVMT EAHHKYDHSE ATGSSSWDIQ NSFRREKLEQ KSPDSKTLQE DSPGVRQRVY ECQECGKSFR QKGSLTLHER IHTGQKPFEC THCGKSFRAK GNLVTHQRIH TGEKPYQCKE CGKSFSQRGS LAVHERLHTG QKPYECAICQ RSFRNQSNLA VHRRVHSGEK PYRCDQCGKA FSQKGSLIVH IRVHTGLKPY ACTQCRKSFH TRGNCILHGK IHTGETPYLC GQCGKSFTQR GSLAVHQRSC SQRLTL.
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.