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1000 results found for “Ubiquitin”
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Name :
CXCL8 Human (1-77)Description:
Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8)
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-327Price :
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Shipped at Room temp
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- sds-page
Description
Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8904 Dalton. The IL-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.sds-page
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
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 8 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
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein has a total Mw of 8.9kDa.
What is the source or expression system of CXCL8 HUMAN (1-77) Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN (1-77) Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.
What is the amino acid sequence of CXCL8 HUMAN (1-77) Protein?
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.
What applications can CXCL8 HUMAN (1-77) Protein be used in?
CXCL8 HUMAN (1-77) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN (1-77) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-77) 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 :
UTI HumanDescription:
Urinary Trypsin Inhibitor-Ulinastatin Human
UTI, Ulinastatin, Urinary Trypsin Inhibitor.
Product # :
PRO-321Price :
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Shipped at Room temp
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Description
Ulinastatin is derived from human urine.
Source
Human Urine.
Formulation
Lyophilized from a (1mg/ml) solution containing no additives.
Biological Activity
Human UTI has an activity of 2350IU/mg.
More Info
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Introduction
Urinary-Trypsin Inhibitor is a glucoprotein proteinase inhibitor which inhibits the activity of trypsin, chymotrypsin, lactate, lipase, hyaluronidase and various pancreatic enzymes. Ulinastatin is effective for acute pancreatitis, chronic recurrent pancreatitis and hemorrhagic, traumatic and endotoxic shocks. Ulinastatin is has strong inhibition effect to various protease, sugar and fat hydrolase. Ulinastatin precursor is proteolytically processed into distinct functioning proteins. Urinary trypsin inhibitor belongs to the superfamily of Kunitz-type protease inhibitors and plays an important role in many physiological and pathological processes. Uristatin gene is located on chromosome 9 in a cluster of lipocalin genes.
High levels of Ulinastatin secretion is an early marker of renal tubular involvement and has radical scavenging activity. Bikunin localizes cell membrane.
Free uristatin and bikunin pass readily into urine and are primarily bound to heavy chains that constitute the proinhibitor form in plasma. UTI has a calculated Mw of approx. 20kDa and 40kDa by SDS-PAGE analysis.
Ulinastatin particularly interacts with ORF3 protein of hepatitis E virus and in charge for enhancing alpha microglobulin export from the hepatocyte. -
Synonyms
UTI, Ulinastatin, Urinary Trypsin Inhibitor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized UTI between 2-8°C, do not freeze. Upon reconstitution UTI 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 UTI in sterile 18MΩ-cm H2O 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.
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Name :
Fibronectin HumanDescription:
Fibronectin Human
Product # :
PRO-448Price :
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Shipped at Room temp
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Description
Human Fibronectin produced purified from Human Plasma having a Molecular Weight of 440kDa.
Source
Human Plasma.
Formulation
The Fibronectin was lyophilized from a non sterile 2mg/ml buffer of 10mM sodium phosphate, pH 7.5 and 0.15M NaCl.
Purity
≥ 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin plays a role in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. Fibronectin consists in two main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the extracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin also takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin should be stored at 4°C between 2-7 days and for future use below -18°C.
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Solubility
We suggest reconstituting the 1mg Fibronectin with a chaotropic agent such as urea at room temperature at a concentration of 0.2mg/ml using sterile water. Let stand 1-2 hours. The recommended concentration is 4M-5M urea.
When using the protein as an attachment factor, wash the urea off after attaching the fibronectin to the growth surface (plate or dish).
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 :
CRTAM HumanDescription:
Cytotoxic and Regulatory T Cell Molecule Human Recombinant
Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.
Product # :
PRO-2247Price :
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Shipped with Ice Packs
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Description
CRTAM produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 278 amino acids (18-287 a.a.) and having a molecular mass of 31.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CRTAM is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CRTAM protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytotoxic and Regulatory T Cell Molecule, also known as CRTAM belongs to the immunoglobulin superfamily which complies with the structural characteristics of the JAM family and is phylogenetically more closely related to nectin-like proteins. CRTAM is implicated in epithelial cell adhesion. Furthermore, CRTAM interacts with CADM1 as well as promotes natural killer (NK) cell cytotoxicity.
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Synonyms
Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.
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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
SLTNHTETIT VEEGQTLTLK CVTSLRKNSS LQWLTPSGFT IFLNEYPALK NSKYQLLHHS ANQLSITVPN VTLQDEGVYK CLHYSDSVST KEVKVIVLAT PFKPILEASV IRKQNGEEHV VLMCSTMRSK PPPQITWLLG NSMEVSGGTL HEFETDGKKC NTTSTLIIHT YGKNSTVDCI IRHRGLQGRK LVAPFRFEDL VTDEETASDA LERNSLSSQD PQQPTSTVSV TEDSSTSEID KEEKEQTTQD PDLTTEANPQ YLGLARKKSG LEHHHHHH.
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 :
Activin A Human PlantDescription:
Activin A Human Recombinant, Plant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-052Price :
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Shipped at Room temp
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Description
Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Activin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin A 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 Activin A 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
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.
What is the source or expression system of Activin A Protein?
Nicotinia
What is the Purity of Activin A Protein?
Activin A Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological functionality of Activin-A Protein will be determined in the future.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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Serological Identification
The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin A.
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 :
HDAC8 HumanDescription:
Histone Deacetylase 8 Human Recombinant
Histone deacetylase 8, HD8, HDAC8, HDACL1, CDA07, RPD3.
Product # :
ENZ-210Price :
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Shipping Method :
Shipped with Ice Packs
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Description
HDAC8 Human Recombinant produced in Sf9 Baculovirus cells, glycosylated polypeptide chain containing 383 amino acids (1-377) and having a molecular mass of 42.6kDa. HDAC8 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The HDAC8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.
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Synonyms
Histone deacetylase 8, HD8, HDAC8, HDACL1, CDA07, RPD3.
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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
MEEPEEPADS GQSLVPVYIY SPEYVSMCDS LAKIPKRASM VHSLIEAYAL HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDDDH PDSIEYGLGY DCPATEGIFD YAAAIGGATI TAAQCLIDGM CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFE RILYVDLDLH HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDGIQDEKY YQICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWQLATLI LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH RIQQILNYIK GNLKHVVHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
APOHDescription:
Apolipoprotein-H Human Recombinant
Beta-2-glycoprotein 1, APC inhibitor, Activated protein C-binding protein, Anticardiolipin cofactor, Apolipoprotein H, Apo-H, Beta-2-glycoprotein I, B2GPI, Beta(2)GPI, APOH, B2G1, BG, B2GP1.
Product # :
CYT-189Price :
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Shipped with Ice Packs
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Description
APOH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (20-345 a.a.) and having a molecular mass of 38.6kDa.APOH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
APOH protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
sds-page
More Info
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Synonyms
Beta-2-glycoprotein 1, APC inhibitor, Activated protein C-binding protein, Anticardiolipin cofactor, Apolipoprotein H, Apo-H, Beta-2-glycoprotein I, B2GPI, Beta(2)GPI, APOH, B2G1, BG, B2GP1.
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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 MGSGRTCPKP DDLPFSTVVP LKTFYEPGEE ITYSCKPGYV SRGGMRKFIC PLTGLWPINT LKCTPRVCPF AGILENGAVR YTTFEYPNTI SFSCNTGFYL NGADSAKCTE EGKWSPELPV CAPIICPPPS IPTFATLRVY KPSAGNNSLY RDTAVFECLP QHAMFGNDTI TCTTHGNWTK LPECREVKCP FPSRPDNGFV NYPAKPTLYY KDKATFGCHD GYSLDGPEEI ECTKLGNWSA MPSCKASCKV PVKKATVVYQ GERVKIQEKF KNGMLHGDKV SFFCKNKEKK CSYTEDAQCI DGTIEVPKCF KEHSSLAFWK TDASDVKPC.
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Background
Apolipoprotein-H Human Recombinant: Unleashing the Potential for Cardiovascular Health
Abstract:
Apolipoprotein-H (Apo-H) is a remarkable protein with diverse functions in lipid metabolism and thrombotic regulation. This research paper provides an in-depth analysis of Apo-H human recombinant, exploring its physiological roles, genetic implications, and potential therapeutic applications. Understanding the intricacies of Apo-H sheds light on its significance in cardiovascular health and highlights its potential as a therapeutic target. This article offers a concise yet comprehensive examination of Apo-H, emphasizing its impact on human well-being.
Introduction:
Cardiovascular health is of utmost importance in preventing and managing cardiovascular diseases. Apo-H, a multifunctional protein involved in lipid metabolism and thrombotic regulation, offers a unique perspective in understanding these processes. This paper explores the multifaceted nature of Apo-H, elucidating its genetic implications and its role as a potential guardian of cardiovascular well-being.
Structure and Function of Apolipoprotein-H:
Apo-H possesses a complex molecular structure, consisting of distinct domains that facilitate interactions with lipoproteins and coagulation factors. It plays a critical role in lipid transport, regulating triglyceride-rich lipoproteins. Additionally, Apo-H contributes to the delicate balance of thrombotic processes through its anticoagulant and fibrinolytic activities.
Genetic Implications of Apolipoprotein-H:
The APOH gene, responsible for encoding Apo-H, exhibits genetic variations that can influence an individual's susceptibility to cardiovascular diseases. Understanding these genetic variations helps identify potential risk factors and therapeutic targets for cardiovascular disorders.
Apolipoprotein-H and Cardiovascular Diseases:
Apo-H has garnered significant attention in the field of cardiovascular diseases, particularly in relation to atherosclerosis and thrombotic events. Its versatility allows modulation of inflammatory responses, maintenance of endothelial function, and regulation of coagulation pathways. Investigating the intricate interplay between Apo-H and cardiovascular processes may yield innovative therapeutic strategies.
Production of Apolipoprotein-H Human Recombinant:
Cutting-edge biotechnological techniques, such as recombinant DNA technology and protein expression systems, enable the production of Apo-H human recombinant. These methods facilitate large-scale production, purification, and characterization of Apo-H, providing opportunities for potential therapeutic applications.
Therapeutic Potential of Apolipoprotein-H Human Recombinant:
Leveraging the therapeutic potential of Apo-H holds promise in cardiovascular interventions. Strategies aimed at enhancing Apo-H expression or function may contribute to lipid homeostasis, prevent thrombotic events, and reduce the risk of cardiovascular diseases.
Conclusion:
Apolipoprotein-H human recombinant represents a fascinating area of research, bridging the realms of lipid metabolism and cardiovascular health. Understanding the genetic implications and cardiovascular protective properties of Apo-H is pivotal in advancing our knowledge and developing novel therapeutic approaches for cardiovascular diseases. Continued investigation into the functions and mechanisms of Apo-H will likely unveil innovative strategies for promoting cardiovascular well-being.
What is the molecular weight/Mw of APOH Protein?
APOH Protein has a total Mw of 38.6kDa.
What is the source or expression system of APOH Protein?
Escherichia Coli.
What is the Purity of APOH Protein?
APOH Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of APOH Protein?
The biological functionality of APOH Protein will be determined in the future.
What is the amino acid sequence of APOH Protein?
MGSSHHHHHH SSGLVPRGSH MGSGRTCPKP DDLPFSTVVP LKTFYEPGEE ITYSCKPGYV SRGGMRKFIC PLTGLWPINT LKCTPRVCPF AGILENGAVR YTTFEYPNTI SFSCNTGFYL NGADSAKCTE EGKWSPELPV CAPIICPPPS IPTFATLRVY KPSAGNNSLY RDTAVFECLP QHAMFGNDTI TCTTHGNWTK LPECREVKCP FPSRPDNGFV NYPAKPTLYY KDKATFGCHD GYSLDGPEEI ECTKLGNWSA MPSCKASCKV PVKKATVVYQ GERVKIQEKF KNGMLHGDKV SFFCKNKEKK CSYTEDAQCI DGTIEVPKCF KEHSSLAFWK TDASDVKPC.
What applications can APOH Protein be used in?
APOH Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOH Protein?
The endotoxin level is minimal, APOH 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 :
ARL4A HumanDescription:
ADP-Ribosylation Factor-Like 4A Human Recombinant
ADP-ribosylation factor-like protein 4A, ARL4A.
Product # :
PRO-895Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARL4A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200) and having a molecular mass of 24.7 kDa.The ARL4A is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ARL4A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ARL4A is related Specifically to ARL6 and ARL7 and belongs to the ARF-like protein (ARL) subfamily of small GTPases. However, unlike ARFs, ARL4 does not activate the cholera toxin ADP-ribosyltranferase. ARL4A takes part in neurogenesis during embryonic development and somitogenesis in the early stages of adult spermatogenesis.
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Synonyms
ADP-ribosylation factor-like protein 4A, ARL4A.
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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 MGNGLSDQTS ILSNLPSFQS FHIVILGLDC AGKTTVLYRL QFNEFVNTVP TKGFNTEKIK VTLGNSKTVT FHFWDVGGQE KLRPLWKSYT RCTDGIVFVV DSVDVERMEE AKTELHKITR ISENQGVPVL IVANKQDLRN SLSLSEIEKL LAMGELSSST PWHLQPTCAI IGDGLKEGLE KLHDMIIKRR KMLRQQKKKR
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 :
IDNK E.Coli, ActiveDescription:
Thermosensitive Gluconokinase E.Coli Recombinant, BioActive
Thermosensitive gluconokinase, Gluconate kinase 1, idnK, D-gluconate kinase thermosensitive, D-gluconate kinase, thermosensitive, ECK4261, gntV, JW4225, b4268
Product # :
PKA-122Price :
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Shipped with Ice Packs
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Description
IDNK Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187) and having a molecular mass of 23.4 kDa.IDNK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDNK solution (1 mg/ml) contains 10% Glycerol, 1mM DTT, 0.15M NaCl and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 80unit/mg. One unit will convert 1.0 umole of D-gluconate to 6-phospho-Dgluconate per minute at pH 8.0 at 37˚C.
More Info
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Introduction
D-gluconate kinase or idnk is a thermosensitive protein, consists of 187 a.a and part of the gluconokinase gntK/gntV protein family. Idnk enhances the conversion of ATP + D-gluconate => ADP + 6-phospho-D-gluconate. Idnk has a crucial part in determination of gender, removal of a certain portion of 9p may result in the making of male to female (reversal of sex), that leads to a female that has the genotype of male X, Y.
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Synonyms
Thermosensitive gluconokinase, Gluconate kinase 1, idnK, D-gluconate kinase thermosensitive, D-gluconate kinase, thermosensitive, ECK4261, gntV, JW4225, b4268
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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 MGSMAGESFI LMGVSGSGKT LIGSKVAALL SAKFIDGDDL HPAKNIDKMS QGIPLSDEDR LPWLERLNDA SYSLYKKNET GFIVCSSLKK QYRDILRKGS PHVHFLWLDG DYETILARMQ RRAGHFMPVA LLKSQFEALE RPQADEQDIV RIDINHDIAN VTEQCRQAVL AIRQNRICAK EGSASDQRCE
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 :
SPA17 HumanDescription:
Sperm Autoantigenic Protein 17 Human Recombinant
CT22, SP17, SP17-1, Sperm surface protein Sp17, Cancer/testis antigen 22, Sperm autoantigenic protein 17, Sperm protein 17, SPA17.
Product # :
PRO-1425Price :
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Description
SPA17 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-151) and having a molecular mass of 19.8kDa. SPA17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SPA17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SPA17 is a protein present at the cell surface. SPA17 was characterized by its participation in the binding of sperm to the zona pellucida of the oocyte. The central portion of SPA17 has carbohydrate binding motifs and likely takes part in cell-cell adhesion functions such as immune cell migration and metastasis.
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Synonyms
CT22, SP17, SP17-1, Sperm surface protein Sp17, Cancer/testis antigen 22, Sperm autoantigenic protein 17, Sperm protein 17, SPA17.
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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 MGSMSIPFSN THYRIPQGFG NLLEGLTREI LREQPDNIPA FAAAYFESLL EKREKTNFDP AEWGSKVEDR FYNNHAFEEQ EPPEKSDPKQ EESQISGKEE ETSVTILDSS EEDKEKEEVA AVKIQAAFRG HIAREEAKKM KTNSLQNEEK EENK.
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 :
ESM1 Human, HEKDescription:
Endothelial Cell-Specific Molecule 1 Human Recombinant, HEK
Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.
Product # :
PRO-2476Price :
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Description
ESM1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-184) containing 175 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 19.5kDa (calculated).
Source
HEK293 cells.
Formulation
ESM1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Endothelial cell-specific molecule 1 (ESM1) is a proteoglycan secreted by endothelial cells (mostly in the human lung and kidney tissues) and its mRNA expression is regulated by inflammatory cytokines. ESM1 has potent implications in lung endothelial cell-leukocyte interactions. In addition, ESM1 expression is detected in various epithelia and in adipocytes. ESM1 is involved in angiogenesis and it also promotes angiogenic sprouting. ESM1 expression is upregulated by TNF alpha, IL1 beta, or lipopolysaccharide and downregulated by IFN gamma. Genetically engineered cells overexpressing ESM1 induce tumor formation, implying that ESM1 might be involved in the pathophysiology of tumor growth in vivo.
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Synonyms
Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. ESM1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
WSNNYAVDCP QHCDSSECKS SPRCKRTVLD DCGCCRVCAA GRGETCYRTV SGMDGMKCGP GLRCQPSNGE DPFGEEFGIC KDCPYGTFGM DCRETCNCQS GICDRGTGKC LKFPFFQYSV TKSSNRFVSL TEHDMASGDG NIVREEVVKE NAAGSPVMRK WLNPR HHHHH 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 :
PFDN6 HumanDescription:
Prefoldin Subunit 6 Human Recombinant
Prefoldin Subunit 6, PFD6, H2-KE2, KE-2, HKE2, HLA class II region expressed gene KE2, MGC70744.
Product # :
PRO-178Price :
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Description
PFDN6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (1-129a.a.) and having a molecular mass of 16.7 kDa. PFDN6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PFDN6 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PFDN6 is a subunit of the heteromeric prefoldin complex that chaperones developing actin and alpha- and beta-tubulin chains until they are transferred to the cytosolic chaperonin containing TCP1 (CCT) complex. PFDN6 binds specifically to cytosolic chaperonin (c-CPN), transfers target proteins to it and bind to developing polypeptide chain to promote folding in a setting where there are many competing pathways for nonnative proteins.
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Synonyms
Prefoldin Subunit 6, PFD6, H2-KE2, KE-2, HKE2, HLA class II region expressed gene KE2, MGC70744.
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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 MAELIQKKLQ GEVEKYQQLQ KDLSKSMSGR QKLEAQLTEN NIVKEELALL DGSNVVFKLL GPVLVKQELG EARATVGKRL DYITAEIKRY ESQLRDLERQ SEQQRETLAQ LQQEFQRAQA AKAGAPGKA
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 :
TIPIN HumanDescription:
TIMELESS Interacting Protein Human Recombinant
TIMELESS Interacting Protein, CSM3 Homolog.
Product # :
PRO-1710Price :
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Description
TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.
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Synonyms
TIMELESS Interacting Protein, CSM3 Homolog.
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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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR
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 :
Activin-A Human ActiveDescription:
Activin-A Human Recombinant, Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-145Price :
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Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CRKL HumanDescription:
V-crk Sarcoma Virus CT10 Oncogene Homolog (Avian)-Like Human Recombinant
Crk-like protein, CRKL.
Product # :
PRO-063Price :
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Description
CRKL Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 323 amino acids (1-303 a.a.) and having a molecular mass of 35.9kDa (Molecular size on SDS-PAGE will appear higher). The CRKL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRKL solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Crk-like protein (CRKL) is a protein kinase containing SH2 and SH3 (src homology) domains which activates the RAS and JUN kinase signaling pathways and transforms fibroblasts in a RAS-dependent manner. CRKL is a substitute of the BCR-ABL tyrosine kinase, it also has a role in fibroblast transformation by BCR-ABL, and has oncogenic potential.
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Synonyms
Crk-like protein, CRKL.
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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 MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRDSSTCPGDYVL SVSENSRVSH YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPM GSVSAPNLPT AEDNLEYVRT LYDFPGNDAE DLPFKKGEIL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPAVS GSPGAAITPL PSTQNGPVFA KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD ENE.
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 :
CRYGS HumanDescription:
Crystallin, Gamma S Human Recombinant
Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.
Product # :
PRO-963Price :
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Description
CRYGS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-178) and having a molecular mass of 23.6 kDa.The CRYGS is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CRYGS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Mammalian crystallins which are water soluble structural proteins located in the vertebrate eye are classified in three forms, labeled alpha, beta and gamma. Crystallins, the primary components of the lens, raise the refractive index of the eye all through the accommodation by creating high-molecular weight aggregates that maintain transparency. CRYGS is a monomer that does not aggregate. CRYGS encodes the most substantial gamma-crystallin in adult eye lens tissue. Gamma-crystallins has a part in cataract formation due to aging or mutations in specific genes,
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Synonyms
Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.
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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 MGSHMSKTGT KITFYEDKNF QGRRYDCDCD CADFHTYLSR CNSIKVEGGT WAVYERPNFA GYMYILPQGE YPEYQRWMGL NDRLSSCRAV HLPSGGQYKI QIFEKGDFSG QMYETTEDCP SIMEQFHMRE IHSCKVLEGV WIFYELPNYR GRQYLLDKKE YRKPIDWGAA SPAVQSFRRI VE
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 :
MIP 1a RatDescription:
Macrophage Inflammatory Protein-1 Alpha Rat Recombinant (CCL3)
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.
Product # :
CHM-343Price :
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Shipped at Room temp
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Description
Macrophage Inflammatory Protein-1 alpha Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7853 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 1 mg/ml solution containing no additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability to chemoattract of rat peritoneal macrophages using a conc. of 60 ng/ml corresponding to a Specific Activity of 16,667IU/mg.More Info
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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 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 Macrophage Inflammatory Protein-1a 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, Ala-Pro-Tyr-Gly-Ala.
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Background
What is the molecular weight/Mw of MIP 1A RAT Protein?
MIP 1A RAT Protein has a total Mw of 7.85kDa.
What is the source or expression system of MIP 1A RAT Protein?
Escherichia Coli.
What is the Purity of MIP 1A RAT Protein?
MIP 1A RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A RAT Protein?
The Activity is calculated by the ability to chemoattract of rat peritoneal macrophages using a conc. of 60 ng/ml corresponding to a Specific Activity of 16,667IU/mg.
What is the amino acid sequence of MIP 1A RAT Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.
What applications can MIP 1A RAT Protein be used in?
MIP 1A RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A RAT Protein?
The endotoxin level is minimal, MIP 1A RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MYL1 HumanDescription:
Myosin Light Chain 1 Human Recombinant
Myosin light chain 1 skeletal muscle isoform, MLC1F, A1 catalytic, Alkali myosin light chain 1, MYL1, MLC3F.
Product # :
PRO-365Price :
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Description
Recombinant Human Ventricular Myosin Light Chain-1 (MYL1) protein has a molecular mass of 25 kDa and is fused to 7 amino acids at N-terminus. The MYL1 protein was affinity purified using anti MYL1 monoclonal antibody 39-15 column.
Source
Escherichia Coli.
Formulation
Human MYL1 in 10mM Tris -HCI, 1mM EDTA PH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Myosin is a hexameric ATPase cellular motor protein, which is composed of 2 heavy chains, 2 non-phosphorylatable alkali light chains, and 2 phosphorylatable regulatory light chains.
MYL1 gene encodes a myosin alkali light chain expressed in fast skeletal muscle. Two transcript variants have been identified for the MYL1 gene. In humans MYL1 is localized to chromosome 2q32.1-qter. The Myl1 locus encodes two alkali myosin light chains- Mlc1f and Mlc3f, from two promoters that are differentially regulated throughout development. The Mlc1f promoter is active in embryonic, fetal and adult fast skeletal muscle while the Mlc3f promoter is upregulated during fetal development and stays on in adult fast skeletal muscle. -
Synonyms
Myosin light chain 1 skeletal muscle isoform, MLC1F, A1 catalytic, Alkali myosin light chain 1, MYL1, MLC3F.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please 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.
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Name :
MYL7 HumanDescription:
Myosin Light Chain 7 Human Recombinant
Myosin light chain 7 regulatory, myosin light polypeptide 7 regulatory, Myosin light chain 2a myosin regulatory light chain 2 atrial isoform, MYL2A, MYLC2A.
Product # :
PRO-1109Price :
Quantity :
Shipping Method :
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Description
MYL7 Human Recombinant produced in E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.0kDa.MYL7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MYL7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MYL7 protein is an atrial isoform of myosin regulatory light chain 2 (MYL2). Myosin is a hexamer containing 4 light chains and 2 heavy chains. MYL7 is mainly expressed in adult atrial muscle.
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Synonyms
Myosin light chain 7 regulatory, myosin light polypeptide 7 regulatory, Myosin light chain 2a myosin regulatory light chain 2 atrial isoform, MYL2A, MYLC2A.
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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 MGSHMASRKA GTRGKVAATK QAQRGSSNVF SMFEQAQIQE FKEAFSCIDQ NRDGIICKAD LRETYSQLGK VSVPEEELDA MLQEGKGPIN FTVFLTLFGE KLNGTDPEEA ILSAFRMFDP SGKGVVNKDE FKQLLLTQAD KFSPAEVEQM FALTPMDLAG NIDYKSLCYI ITHGDEKEE
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 :
SH3GL2 HumanDescription:
SH3-domain GRB2-like 2 Human Recombinant
Endophilin-A1, EEN-B1, Endophilin-1, SH3 domain protein 2A, SH3 domain-containing, GRB2-like protein 2, SH3GL2, CNSA2, SH3D2A, SH3P4.
Product # :
PRO-1083Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SH3GL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (1-352 a.a) and having a molecular mass of 42.5kDa.SH3GL2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SH3GL2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SH3-domain GRB2-like 2 (SH3GL2) is a member of the endophilin family. SH3GL2 contains a BAR domain and a SH3 domain. Members of the BAR domain protein superfamily are crucial elements of cellular traffic. Endophilins have a major function in synaptic vesicle endocytosis (SVE), receptor trafficking and apoptosis, and in other processes which require remodeling of the membrane structure. SH3GL2 is a novel tumor suppressor gene in laryngeal squamous cell carcinoma (LSCC), which induces apoptosis of tumor cells by regulating intra-cellular signal transduction networks. SH3GL2 is implicated in synaptic vesicle endocytosis. SH3GL2 is found in the brain, mainly in frontal cortex, and at high level in the fetal cerebellum.
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Synonyms
Endophilin-A1, EEN-B1, Endophilin-1, SH3 domain protein 2A, SH3 domain-containing, GRB2-like protein 2, SH3GL2, CNSA2, SH3D2A, SH3P4.
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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 MGSHMSVAGL KKQFHKATQK VSEKVGGAEG TKLDDDFKEM ERKVDVTSRA VMEIMTKTIE YLQPNPASRA KLSMINTMSK IRGQEKGPGY PQAEALLAEA MLKFGRELGD DCNFGPALGE VGEAMRELSE VKDSLDIEVK QNFIDPLQNL HDKDLREIQH
HLKKLEGRRL DFDYKKKRQG KIPDEELRQA LEKFDESKEI AESSMFNLLE MDIEQVSQLS ALVQAQLEYH KQAVQILQQV TVRLEERIRQ ASSQPRREYQ PKPRMSLEFP TGDSTQPNGG LSHTGTPKPS GVQMDQPCCR ALYDFEPENE GELGFKEGDI ITLTNQIDEN WYEGMLHGHS
GFFPINYVEI LVALPH.
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 :
DnaJ E.ColiDescription:
DnaJ (HSP40) E.Coli Recombinant
HSP-40, HSP40, DnaJ, DNAJB1, HSPF1, Hdj1, Chaperone protein dnaJ, Heat shock protein J, groP, b0015, JW0014.
Product # :
HSP-007Price :
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Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Dna-J produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids and having a molecular mass of 41.1 kDa.
Source
Escherichia Coli.
Formulation
The DnaJ contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DnaJ, Heat shock protein, functions in association with DnaK(Hsp70) molecular chaperone to facilitate protein folding. p70 chaperone. DnaJ plays a key role in the chaperone reaction by stimulating the ATPase activity and activating the substrate binding of Hsp70. DnaJ consists of four domains that are N-terminal 76 amino acid J-domain, G/F domain, zinc-binding cystein rich CR-domain, C-terminal CTD-domain and they are conserved to various degrees among the homologues.
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Synonyms
HSP-40, HSP40, DnaJ, DNAJB1, HSPF1, Hdj1, Chaperone protein dnaJ, Heat shock protein J, groP, b0015, JW0014.
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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
MAKQDYYEIL GVSKTAEEHE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDSQKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYNMELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQQTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAPAGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG PTGEHNSPRSKSFFDGVKKF FDDLTR.
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 :
SH3GLB2 HumanDescription:
SH3-domain GRB2-like endophilin B2 Human Recombinant
PP6569, PP9455, Endophilin-B2, KIAA1848, SH3 domain-containing GRB2-like protein B2.
Product # :
PRO-1287Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SH3GLB2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (1-395a.a.) and having a molecular mass of 46.4 kDa. SH3GLB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SH3GLB2 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Endophilin-B2 (SH3GLB2) belongs to the endophilin B subgroup. The endophilins comprise a family of proteins that relates with amphiphysin, synaptojanin and dynamin and are involved in presynaptic vesicle trafficking at nerve terminals.The expression patterns of the endophilins are coherent with their cellular functions at the neuronal synapse. SH3GLB2 is ubiquitously expressed however presents highest levels in brain, adult lung, ovary, and spinal cord.Low levels of SH3GLB2 are found in Down syndrome and reflect brain dysgenesis.
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Synonyms
PP6569, PP9455, Endophilin-B2, KIAA1848, SH3 domain-containing GRB2-like protein B2.
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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 MGSMDFNMKK LASDAGIFFT RAVQFTEEKF GQAEKTELDA HFENLLARAD STKNWTEKIL RQTEVLLQPN PSARVEEFLY EKLDRKVPSR VTNGELLAQY MADAASELGP TTPYGKTLIK VAEAEKQLGA AERDFIHTAS ISFLTPLRNF LEGDWKTISK ERRLLQNRRL DLDACKARLK KAKAAEAKAT TVPDFQETRP RNYILSASAS ALWNDEVDKA EQELRVAQTE FDRQAEVTRL LLEGISSTHV NHLRCLHEFV KSQTTYYAQC YRHMLDLQKQ LGRFPGTFVG TTEPASPPLS STSPTTAAAT MPVVPSVASL APPGEASLCL EEVAPPASGT RKARVLYDYE AADSSELALL ADELITVYSL PGMDPDWLIG ERGNKKGKVP VTYLELLS.
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 :
ARL4D HumanDescription:
ADP-Ribosylation Factor-Like 4D Human Recombinant
ADP-ribosylation factor-like 4D, ADP-ribosylation factor-like protein 4L, ARF4L, ARL6.
Product # :
PRO-953Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARL4D Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-201) and having a molecular mass of 24.3 kDa.ARL4D is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ARL4D solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ARL4D is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). ARL4D takes part in membrane-associated intracellular trafficking. Mutations in this gene is linked to Bardet-Biedl syndrome (BBS).
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Synonyms
ADP-ribosylation factor-like 4D, ADP-ribosylation factor-like protein 4L, ARF4L, ARL6.
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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 MGNHLTEMAP TASSFLPHFQ ALHVVVIGLD SAGKTSLLYR LKFKEFVQSV PTKGFNTEKI RVPLGGSRGI TFQVWDVGGQ EKLRPLWRSY TRRTDGLVFV VDAAEAERLE EAKVELHRIS RASDNQGVPV LVLANKQDQP GALSAAEVEK RLAVRELAAA TLTHVQGCSA VDGLGLQQGL ERLYEMILKR KKAARGGKKR R
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 :
ID2 HumanDescription:
Inhibitor of DNA Binding 2 Human Recombinant
DNA-binding protein inhibitor ID-2, bHLHb26, GIG8, ID2A, ID2H, MGC26389, Class B basic helix-loop-helix protein 26, Inhibitor of DNA binding 2.
Product # :
PRO-1383Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
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Description
ID2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-134 a.a.) and having a molecular mass of 17kDa. ID2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
ID2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Inhibitor of DNA Binding 2 (ID2) is a part of the inhibitor of DNA binding family, whose members are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative way by suppressing their heterodimerization partners through the HLH domains. ID2 play a role in negatively regulating cell differentiation and may be an inhibitor of tissue-specific gene expression.
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Synonyms
DNA-binding protein inhibitor ID-2, bHLHb26, GIG8, ID2A, ID2H, MGC26389, Class B basic helix-loop-helix protein 26, Inhibitor of DNA binding 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 MKAFSPVRSV RKNSLSDHSL GISRSKTPVD DPMSLLYNMN DCYSKLKELV PSIPQNKKVS KMEILQHVID YILDLQIALD SHPTIVSLHH QRPGQNQASR TPLTTLNTDI SILSLQASEF PSELMSNDSK ALCG.
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.