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Name :
EGFPDescription:
Enhanced Green Fluorescent Protein Recombinant
Green fluorescent protein, GFP.
Product # :
PRO-1606Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant EGFP produced in E.coli cells is a single non-glycosylated protein containing 239 amino acid chain and having a molecular mass of 26.9kDa. EGFP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGFP was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
GFP, also known as Green Fluorescent Protein, is a protein produced by the jellyfish (Aequorea Victoria) that produces bioluminescence in the green zone of the noticeable spectrum. Green Fluorescent Protein is a useful and ubiquitous instrument for producing chimeric proteins, where it functions as a fluorescent protein tag. GFP is expressed in most known cell types and is used as a noninvasive fluorescent marker in living cells and organisms. Green Fluorescent Protein permits a broad range of applications where it has functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions. Enhanced GFP (eGFP) has F64L and S65T mutations, which make GFP show increased fluorescence and fold more efficiently under 370.
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Synonyms
Green fluorescent protein, GFP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGFP although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution EGFP should be stored at 40C between 2-7 days and for future use below -180C.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 EGFP in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH KLEYNYNSHN VYIMADKQKN GIKVNFKIRH NIEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMV LLEFVTAAGI TLGMDELYK
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 :
SERPINH1 HumanDescription:
Heat Shock 47kDa Human Recombinant
HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.
Product # :
HSP-047Price :
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Shipped with Ice Packs
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Description
Recombinant Human HSP47 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (18-418 a.a.) and having a molecular mass of 48.9 kDa. HSP47 human recombinant is fused to a 38 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.
Source
Escherichia Coli.
Formulation
The SERPINH1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SERPINH1 is part of the serpin superfamily of serine proteinase inhibitors. SEPINH1 expression is induced by heat shock. HSP47 localizes to the endoplasmic reticulum lumen and binds collagen therefore it is a molecular chaperone which takes part in the maturation of collagen molecules, facilitating the folding and assembly of procollagen molecules, retaining unfolded molecules within the ER, and assisting the transport of correctly folded-molecules from the ER to Golgi apparatus. Autoantibodies to HSP47 protein have been found in rheumatoid arthritis. SERPINH1 binds specifically to collagen and acts as a chaperone in the biosynthetic pathway of collagen.
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Synonyms
HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAA EVKKPAAAAA PGTAEKLSPK AATLAERSAG LAFSLYQAMA KDQAVENILV SPVVVASSLG LVSLGGKATT ASQAKAVLSA EQLRDEEVHA GLGELLRSLS NSTARNVTWK LGSRLYGPSS VSFADDFVRS SKQHYNCEHS KINFRDKRSA LQSINEWAAQ TTDGKLPEVT KDVERTDGAL LVNAMFFKPH WDEKFHHKMV DNRGFMVTRS YTVGVMMMHR TGLYNYYDDE KEKLQIVEMP LAHKLSSLII LMPHHVEPLE RLEKLLTKEQ LKIWMGKMQK KAVAISLPKG VVEVTHDLQK HLAGLGLTEA IDKNKADLSR MSGKKDLYLA SVFHATAFEL DTDGNPFDQD IYGREELRSP KLFYADHPFI FLVRDTQSGS LLFIGRLVRP KGDKMRDEL.
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 :
BMP 7 Human, HisDescription:
Bone Morphogenetic Protein-7 Human Recombinant, His Tag
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
Product # :
CYT-629Price :
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Shipped with Ice Packs
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Description
BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
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Synonyms
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
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Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK
Abstract:
Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.8kDa.
What is the source or expression system of BMP7 Protein?
Escherichia Coli.
What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.
What is the amino acid sequence of BMP7 Protein?
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 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 :
PPIL1 HumanDescription:
Peptidylprolyl Isomerase (Cyclophilin)-Like 1 Human Recombinant
Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIL-1, CYPL1, hCyPX, MGC678, PPIase, CGI-124, PPIL1.
Product # :
ENZ-388Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PPIL1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-166) and having a molecular mass of 19.3 kDa. PPIL1 is fused to 8 amino acid His Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PPIL1 solution containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.sds-page
More Info
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Introduction
PPIL1 belongs to the cyclophilin family of peptidylprolyl isomerases (PPIases).
The cyclophilins are a well conserved, ubiquitous family, members of which take an significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 protein increases the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. PPIL1 is a novel molecular target for colon-cancer therapy. -
Synonyms
Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIL-1, CYPL1, hCyPX, MGC678, PPIase, CGI-124, PPIL1.
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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
MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLEHH 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 :
CoV-2 OmicronDescription:
Coronavirus 2019 Omicron Full Length Recombinant
Product # :
SARS-059Price :
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Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein contains the Omicron Covid-19 full-length nucleprotein, fused to 6xHis tag at N-terminal migrating at 48 kDa.
Source
Escherichia Coli.
Formulation
CoV-2 Omicron protein solution (2.18mg/ml) is supplied in PBS and 25mM K2CO3.
Purity
Protein is >95% pure as determined SDS-PAGE.
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
On November 2021, WHO designated a variant of concern, named Omicron. Omicron has several mutations that may have an impact on how it behaves (how easily it spreads, the severity of illness). -
Physical Appearance
Sterile Filtered clear solution.
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Stability
Protein is shipped on ice packs. Upon arrival, Store at -20°C.
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Amino Acid Sequence
HMSDNGPQNQ RNALRITFGG PSDSTGSNQN GEARSKQRRP QGLPNNTASW FTALTQHGKE DLKFPRGQGV PINTNSSPDD QIGYYRRATR RIRGGDGKMK ELSPRWYFYY LGTGPEAGLP YGANKDGIIW VATEGALNTP KDHIGTRNPA NNAAIVLQLP QGTTLPKGFY AEGSRGGSQA SSRSSSRSRN SSRNSTPGSS KRTSPARMAG NGGDAALALL LLDRLNQLES KMSGKGQQQQ GQTVTKKSAA EASKKPRQKRT ATKAYNVTQA FGRRGPEQTQ GNFGDQELIR QGTDYKHWPQ IAQFAPSASA FFGMSRIGME VTPSGTWLTY TGAIKLDDKD PNFKDQVILL NKHIDAYKTF PPTEPKKDKK KKADETQALP QRQKKQQTVT LLPAADLDDF SKQLQQSMSS ADSTQA
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 :
BivalirudinDescription:
Bivalirudin
Product # :
PRO-357Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The active of Bivalirudin substance is a synthetic 20 amino acid peptide. The amino acid sequence is Phe-Pro-Arg-Pro-Gly-Gly-Gly-Gly- Asn-Gly-Asp-Phe-Glu-Glu-Ile- Pro-Glu-Glu-Tyr-Leu. The Mw is 2180 dalton.
Formulation
The protein (1mg/ml) was lyophilized with 0.5mg Manntiol and sodium hydroxide 50µg pH-5.5.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Bivalirudin directly inhibits thrombin by specifically binding as well to the catalytic site and to the anion-binding exosite of circulating and clot-bound thrombin. Bivalirudin is a specific and reversible direct thrombin inhibitor.
Thrombin, which is a serine protease, plays a central role in the thrombotic process; it cleaves fibrinogen into fibrin monomers and activates Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked structure which stabilizes the thrombus. Thrombin also activates Factors V and VIII, which promotes further thrombin generation, activates platelets, stimulating aggregation and granule release. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bivalirudin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bivalirudin 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 Bivalirudin 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 :
s100bb BovineDescription:
s100bb Bovine homodimer
Product # :
PRO-2796Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
s100bb Bovine is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.
Source
Bovine brain tissue.
Formulation
s100bb was lyophilized from 5mM Tris-HCl, pH 7.5, 2mM EDTA and 5mM 2-mercaptoethanol.
Purity
Greater than 95.0% .
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized s100bb homodimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution s100bb 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 s100bb in sterile 18MΩ-cm H2O containing 5mM 2- mercaptoethanol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
S100BB, a member of the S100 family of proteins, is a calcium-binding protein that plays a significant role in various cellular processes, particularly in the central nervous system (CNS). Initially identified as a brain-specific protein, S100BB has captured the attention of researchers due to its involvement in neurological signaling, brain development, and its potential implications in neurological disorders. This research delves into the enigmatic world of S100BB, aiming to uncover its diverse functions, regulatory mechanisms, and its relevance in health and disease.
Discovery and Structural Insights:
S100BB was first discovered in the brain, primarily localized in astrocytes, a type of glial cell in the CNS. Structurally, S100BB is characterized by its EF-hand motifs, allowing it to bind calcium ions, a property crucial for its function. These calcium-binding abilities enable S100BB to participate in intricate cellular signaling pathways, making it a vital player in the dynamic communication within the CNS.
Neurological Signaling and Plasticity:
Within the CNS, S100BB has been implicated in neuronal signaling and synaptic plasticity. It interacts with several target proteins, modulating their activities and influencing processes like neurotransmitter release and neuronal differentiation. Furthermore, S100BB participates in the regulation of intracellular calcium levels, a key factor in neuronal excitability and synaptic transmission. Understanding these roles is vital for unraveling the complexities of neurological function and plasticity.
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 :
NAIF1 HumanDescription:
Nuclear Apoptosis Inducing Factor 1 Human Recombinant
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
Product # :
PRO-1978Price :
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Shipped with Ice Packs
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Description
NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.
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Synonyms
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
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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 MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.
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 :
Streptavidin-NCDescription:
Streptavidin-NC Recombinant
Product # :
PRO-338Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Streptavidin-NC produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 24kDa. Streptavidin-NC is engineered to bind to nitrocellulose.
Source
Escherichia Coli.
Formulation
The sterile solution contains 10mM K2HPO4-KH2PO4, pH 7.3.
Purity
Greater than 93.0% as determined by SDS-PAGE.
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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Physical Appearance
Sterile Liquid formulation.
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Stability
Streptavidin-NC although stable at 4°C for 3 weeks, should be stored below -18°C. 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 :
ITGB4 HumanDescription:
Integrin Beta 4 Human Recombinant
Integrin beta-4, GP150, CD104, ITGB4, Integrin Subunit Beta 4, CD104 Antigen, Integrin, Beta 4, Integrin Beta-4.
Product # :
PRO-2528Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ITGB4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 691 amino acids (28-710a.a.) and having a molecular mass of 77.5kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ITGB4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ITGB4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ITGB4 (integrin beta-4 isoform 1) belongs to the Integrin beta family. ITGB4 forms noncovalent heterodimers with Integrin alpha 6 and takes part in the formation of epithelial hemidesmosomes. ITGB4 has a vital structural role in the hemidesmosome of epithelial cells and is needed for the regulation of keratinocyte motility & polarity. ITGB4 leans towards the association with alpha 6 subunit and is expected to take a key role in the biology of invasive carcinoma.
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Synonyms
Integrin beta-4, GP150, CD104, ITGB4, Integrin Subunit Beta 4, CD104 Antigen, Integrin, Beta 4, Integrin Beta-4.
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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
NRCKKAPVKS CTECVRVDKD CAYCTDEMFR DRRCNTQAEL LAAGCQRESI VVMESSFQIT EETQIDTTLR RSQMSPQGLR VRLRPGEERH FELEVFEPLE SPVDLYILMD FSNSMSDDLD NLKKMGQNLA RVLSQLTSDY TIGFGKFVDK VSVPQTDMRP EKLKEPWPNS DPPFSFKNVI SLTEDVDEFR NKLQGERISG NLDAPEGGFD AILQTAVCTR DIGWRPDSTH LLVFSTESAF HYEADGANVL AGIMSRNDER CHLDTTGTYT QYRTQDYPSV PTLVRLLAKH NIIPIFAVTN YSYSYYEKLH TYFPVSSLGV LQEDSSNIVE LLEEAFNRIR SNLDIRALDS PRGLRTEVTS KMFQKTRTGS FHIRRGEVGI YQVQLRALEH VDGTHVCQLP EDQKGNIHLK PSFSDGLKMD AGIICDVCTC ELQKEVRSAR CSFNGDFVCG QCVCSEGWSG QTCNCSTGSL SDIQPCLREG EDKPCSGRGE CQCGHCVCYG EGRYEGQFCE YDNFQCPRTS GFLCNDRGRC SMGQCVCEPG WTGPSCDCPL SNATCIDSNG GICNGRGHCE CGRCHCHQQS LYTDTICEIN YSAIHPGLCE DLRSCVQCQA WGTGEKKGRT CEECNFKVKM VDELKRAEEV VVRCSFRDED DDCTYSYTME GDGAPGPNST VLVHKKKDCP PGSLEHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Troponin C-I-T HumanDescription:
Cardiac Troponin C-I-T Complex Human Recombinant
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Product # :
PRO-344Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Cardiac Troponin C-I-T complex produced in E.Coli is a single, non-glycosylated, polypeptide chain having the Molar ratio on cTnC to cTnI to cTnT of 1:1:1. Mw is approximately 90kDa.The Cardiac Troponin C-I-T complex is purified by proprietary chromatographic techniques
Source
Escherichia Coli.
Formulation
Human Cardiac Troponin C-I-T complex solution contains 500 mM NaCl, 20mM Tris-HCl, 4mM CaCl2, 4mM MgCl2and 60 mM B-mercaptoethanol, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
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Physical Appearance
Sterile Filtered colourless liquid formualtion.
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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. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TTC33 HumanDescription:
Tetratricopeptide Repeat Domain 33 Human Recombinant
Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.
Product # :
PRO-1217Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TTC33 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-262) and having a molecular mass of 31.8 kDa.TTC33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TTC33 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Tetratricopeptide repeat protein 33 (TTC33) is comprised of 3 TPR repeats.
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Synonyms
Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.
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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
MGSSHHHHHH SSGLVPRGSH MGS MASFGWK RKIGEKVSKV TSQQFEAEAA DEKDVVDNDE GNWLHAIKRR KEILLEGCAE KSKQLKDEGA SLAENKRYRE AIQKWDEALQ LTPNDATLYE MKSQVLMSLH EMFPAVHAAE MAVQQNPHSW ESWQTLGRAQ LGLGEIILAI RSFQVALHIY
PMNPEIWKED LSWARTLQEQ QKVAQRIKKS EAPAEVTHFS PKSIPDYDFE SDEIVAVCAA IAEKEKTVSA NKTMVIVSAS GAIETVTEKE DGATPPDGSV FIKAR
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 :
PTEN Human, HisDescription:
Phosphatase and Tensin homolog Human Recombinant, His Tag
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN, EC 3.1.3.67, EC 3.1.3.16, EC 3.1.3.48, Phosphatase and tensin homolog, Mutated in multiple advanced cancers 1, PTEN, MMAC1, TEP1, BZS, MHAM, PTEN1, 10q23del, MGC11227.
Product # :
PRO-712Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PTEN 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 423 amino acids (1- 403 a.a.) and having a molecular mass of 49.3kDa.The PTEN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PTEN solution contains 20mM Tris-HCl buffer (pH 8.0), 1mM EDTA, 2mM DTT, 100mM NaCl, and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
PTEN, a tumor suppressor, has been implicated in a large number of human tumors and is conserved from humans to worms. PTEN has a tensin like domain and a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. Characterization of PTEN protein showed that it is a phosphatase that acts on proteins and on 3-phosphorylated phosphoinositides, and can therefore modulate signal transduction pathways that involve lipid second messengers. In contrast to most of the protein tyrosine phosphatases, PTEN preferentially dephosphorylates phosphoinositide substrates. PTEN negatively regulates intracellular levels of phosphatidylinositol-3,4,5-trisphosphate in cells and acts as a tumor suppressor by negative regulation of AKT/PKB signaling pathway. Recent results indicate that at least part of its role is to regulate the activity of the serine/threonine kinase AKT/PKB, and thus influence cell survival signaling.
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Synonyms
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN, EC 3.1.3.67, EC 3.1.3.16, EC 3.1.3.48, Phosphatase and tensin homolog, Mutated in multiple advanced cancers 1, PTEN, MMAC1, TEP1, BZS, MHAM, PTEN1, 10q23del, MGC11227.
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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).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA AIHCKAGKGR TGVMICAYLL HRGKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY LLKNHLDYRP VALLFHKMMF ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKFMY FEFPQPLPVC GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT VEEPSNPEAS SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHTQI TKV.
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Patent Protected Countries
The Sale of recombinant Human PTEN by ProSpec is prohibited in the following countries: United States, Japan, Australia, Canada, Austria, Belgium, Denmark, Finland, France, Germany, Ireland, Italy, Liechtenstein, Luxembourg, Netherlands, Portugal, Spain, Sweden, Switzerland and UK.
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 :
Kisspeptin-10Description:
Kisspeptin-10
Product # :
HOR-044Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Kisspeptin-10 Synthetic is a single, non-glycosylated polypeptide chain containing 10 amino acids, having a molecular mass of 1302 Dalton and a Molecular formula of C63H83N17O14 .
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Kisspeptin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kisspeptin-10 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 Kisspeptin-10 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2.
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Background
Kisspeptin-10, a peptide derived from the Kisspeptin gene (KISS1), has emerged as a key player in the regulation of reproductive physiology. The peptide is known for its potent ability to stimulate the release of gonadotropin-releasing hormone (GnRH), a crucial factor in the control of the hypothalamic-pituitary-gonadal axis. The pivotal role of kisspeptin-10 in orchestrating the onset of puberty and the regulation of the menstrual cycle highlights its significance in reproductive health. This research aims to delve into the multifaceted functions of kisspeptin-10, shedding light on its physiological roles and potential applications in reproductive disorders.
The primary objective of this study is to comprehensively explore the effects of kisspeptin-10 on the reproductive system. In vitro and in vivo assays will be conducted to investigate the impact of kisspeptin-10 on GnRH release and subsequent gonadotropin secretion. The interactions between kisspeptin-10 and its receptor, G protein-coupled receptor 54 (GPR54), will be explored using binding assays, potentially unraveling novel signaling pathways activated by this interaction.
The second objective is to investigate the potential therapeutic applications of kisspeptin-10 in reproductive disorders. Clinical studies and animal models will be utilized to assess the efficacy of kisspeptin-10 in stimulating ovulation, particularly in cases of infertility caused by hypothalamic dysfunction. Furthermore, the potential of kisspeptin-10 in regulating conditions like polycystic ovary syndrome (PCOS) and hypogonadotropic hypogonadism will be explored.
The third objective is to elucidate the molecular mechanisms underlying the actions of kisspeptin-10. Transcriptomic and proteomic analyses will be employed to identify genes and proteins regulated by kisspeptin-10 stimulation. This information could reveal novel downstream effectors of kisspeptin-10 signaling, contributing to a more comprehensive understanding of its role in reproductive physiology.
By delving into the complexities of kisspeptin-10, this research aims to provide insights into its multifunctional roles in reproductive health and expand its potential therapeutic applications. The findings from this study may pave the way for the development of targeted interventions for reproductive disorders, potentially improving the quality of life for individuals affected by these conditions.
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 :
NT-proBNP CanineDescription:
NT-Pro-B-type Natriuretic Protein Canine Recombinant
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Product # :
CYT-1223Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NT-proBNP Canine produced in E.coli is a single, non-glycosylated polypeptide chain (1-85 a.a) containing 101 a.a and having a molecular mass of 10,545 Dalton. NT-proBNP is fused with a 16 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NT-proBNP was lyophilized from 10mM potassium phosphate, pH 7.4 and 150 mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NT-proBNP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NT-Pro B-type Natriuretic Protein 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 NT-proBNP in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
N-terminal pro-brain natriuretic peptide, or NT-proBNP, has emerged as a significant biomarker in cardiovascular medicine, providing crucial insights into heart function and aiding in the diagnosis and management of heart-related conditions. This peptide, released in response to cardiac stress, reflects the heart's intricate signaling mechanisms and physiological responses. The study of NT-proBNP, especially in its recombinant form, has not only deepened our understanding of heart diseases but has also led to the development of advanced diagnostic tools and potential therapeutic interventions. This research delves into the world of NT-proBNP Recombinant Protein, exploring its biochemical intricacies, physiological roles, and its profound impact on cardiovascular healthcare.
Structural and Molecular Complexity of NT-proBNP:
NT-proBNP, derived from proBNP through enzymatic cleavage, is a stable peptide fragment. It acts as a precursor to the biologically active B-type natriuretic peptide (BNP) hormone. Understanding the molecular structure and processing of NT-proBNP is essential for unraveling the regulatory mechanisms governing its release and its significance in cardiovascular physiology.
Physiological Significance in Heart Function:
BNP and its precursor, NT-proBNP, play pivotal roles in cardiac homeostasis. They are secreted by ventricular myocardial cells in response to increased wall stress, primarily due to volume and pressure overload. Elevated levels of NT-proBNP serve as a sensitive indicator of heart failure, reflecting the heart's struggle to maintain effective circulation. Monitoring NT-proBNP levels aids clinicians in diagnosing heart failure, assessing its severity, and guiding therapeutic strategies, ultimately improving patient outcomes.
Diagnostic Applications and Clinical Relevance:
NT-proBNP assays, often utilizing recombinant NT-proBNP proteins, have become cornerstones in cardiovascular diagnostics. Elevated levels of NT-proBNP are indicative of heart failure, providing vital information for early intervention and personalized treatment plans. Moreover, the peptide's utility extends to predicting cardiovascular events, aiding in risk stratification among individuals with or at risk of heart diseases. The incorporation of NT-proBNP testing into clinical practice has significantly enhanced the accuracy and timeliness of cardiovascular disease diagnosis.
Potential Therapeutic Implications:
Research into NT-proBNP’s regulatory pathways has opened avenues for therapeutic interventions. Targeted therapies aimed at modulating the BNP system are under investigation, offering potential strategies for managing heart failure and related conditions. By understanding the complex interplay between NT-proBNP, its receptor systems, and cardiac function, researchers are exploring novel therapies to optimize cardiovascular health.
NT-proBNP Recombinant Protein, with its intricate involvement in cardiac physiology and its applications in diagnostics and potential therapeutics, stands as a beacon of hope in the realm of cardiovascular medicine. Its role as a diagnostic marker not only aids in early disease detection but also empowers clinicians to tailor treatments, improving patient outcomes and quality of life. As research continues to unravel the complexities of NT-proBNP, it holds the promise of not only enhancing our understanding of heart diseases but also shaping the future of cardiovascular healthcare. This research underscores the vital role of NT-proBNP in cardiovascular medicine, emphasizing its potential to transform the landscape of heart disease diagnosis and treatment.
What is the molecular weight / Mw of NT-proBNP Canine?
NT-proBNP Canine has a total Mw of 10,545 Da.
What is the source or expression system of NT-proBNP Canine?
Escherichia Coli.
What is the Purity of NT-proBNP Canine?
NT-proBNP Canine is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of NT-proBNP Canine?
The biological functionality of NT-proBNP Canine will be determined in the future.
What is the amino acid sequence of NT-proBNP Canine?
NT-proBNP Canine Protein is composed from 16 amino acids.
What applications can NT-proBNP Canine be used in?
NT-proBNP Canine can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for NT-proBNP Canine?
The endotoxin level is minimal, NT-proBNP Canine 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 :
ACVR1 HumanDescription:
Activin A Receptor Type 1 Human Recombinant
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
Product # :
CYT-1140Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
ACVR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (21-123a.a.) and having a molecular mass of 38.4kDa. ACVR1 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ACVR1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Activin A Receptor Type 1 (ACVR1) is a member of TGF-beta serine/threonine kinase receptor family. ACVR1 forms a receptor complex contains2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate,bind and activate SMAD transcriptional regulators. ACVR1 takes part in left-right pattern formation during embryogenesis and is also essential in the BMP pathway which is responsible for the development and repair of the skeletal system.ACVR1 is linked to Fibrodysplasia Ossificans Progressiva which isknown for the formation of heterotopic bone throughout the body.
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Synonyms
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
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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
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH. -
Background
Functional Implications and Therapeutic Prospects of Activin A Receptor Type 1 Human Recombinant
1. Abstract
This study illuminates the functional roles and potential therapeutic applications of Activin A Receptor Type 1 Human Recombinant (ACVR1), a crucial protein in the TGF-beta superfamily signaling pathway. Through a comprehensive review of its structure, signaling mechanism, biological functions, and disease associations, this paper aims to elucidate the current understanding of ACVR1 and its potential therapeutic implications in various disease states.
2. Introduction
The Activin A Receptor Type 1 Human Recombinant, abbreviated as ACVR1, is a receptor protein vital for transmitting cellular signals in the Transforming Growth Factor-beta (TGF-beta) superfamily pathway. Known to play pivotal roles in organogenesis, bone growth, and cell differentiation, the ACVR1 and its functions present vast therapeutic potential.
3. Structure and Signaling of ACVR1
ACVR1 is a transmembrane serine/threonine kinase receptor, characterized by an extracellular ligand-binding domain and an intracellular kinase domain for signal transduction. Binding of ligands such as Activin A leads to the formation of heteromeric complexes with type II receptors, triggering phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVR1
Being a part of the TGF-beta superfamily signaling pathway, ACVR1 is implicated in a broad spectrum of biological processes. It is crucial for embryonic development, cellular proliferation, differentiation, apoptosis, and homeostasis. It also plays a significant role in bone morphogenesis, contributing to skeletal patterning and growth.
5. ACVR1 in Disease Pathology
The dysregulation of ACVR1 has been associated with various pathological conditions, including Fibrodysplasia Ossificans Progressiva (FOP), a rare genetic disorder characterized by progressive ossification of soft tissues. Mutations in ACVR1 lead to enhanced BMP signaling, causing aberrant bone formation. This highlights the critical role of ACVR1 in skeletal homeostasis and disease.
6. Therapeutic Potential of ACVR1
Given the central role of ACVR1 in cellular signaling and its association with disease, it presents a promising target for therapeutic intervention. Strategies to modulate ACVR1 signaling could potentially ameliorate symptoms of diseases like FOP, offering promising avenues for novel therapeutic approaches.
7. Conclusion and Future Perspectives
While our understanding of ACVR1's functional roles has expanded significantly over the years, much remains to be elucidated. Further research into the precise molecular mechanisms of ACVR1 and its pathway will pave the way for therapeutic advances, enhancing our capability to combat various diseases.
What is the molecular weight / Mw of ACVR1 Protein?
ACVR1 Protein has a total Mw of 38.4kDa.
What is the source or expression system of ACVR1 Protein?
Sf9, Baculovirus cells.
What is the Purity of ACVR1 Protein?
ACVR1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVR1 Protein?
The biological functionality of ACVR1 Protein will be determined in the future.
What is the endotoxin level for ACVR1 Protein?
The endotoxin level is minimal, ACVR1 Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACVR1 Protein?
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
What applications can ACVR1 Protein be used in?
ACVR1 Protein can probably be used in western blot, ELISA and Lateral Flow
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 :
CD105 Human, Sf9Description:
Endoglin Human Recombinant, Sf9
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Product # :
CYT-389Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.More Info
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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities. -
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 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 CD-105 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
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Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 90kDa.
What is the source or expression system of CD105 Protein?
Sf9 Insect Cells.
What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.
What is the amino acid sequence of CD105 Protein?
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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 :
CALM BovineDescription:
Calmodulin Bovine
Calmodulin, CaM, CALM.
Product # :
PRO-2800Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- source
- formulation
- purity
- More Info
Source
Bovine brain tissue.
Formulation
CALM was lyophilized with 2mM EDTA.
Purity
Greater than 95.0%.
More Info
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Synonyms
Calmodulin, CaM, CALM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin 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 CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Biochemical and immunochemical investigations.
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Background
Role in Muscle Contraction and Relaxation:
In muscle cells, calmodulin plays a pivotal role in the regulation of contraction and relaxation. It interacts with myosin light-chain kinase during muscle contraction, initiating the process of cross-bridge cycling. Conversely, during muscle relaxation, calmodulin activates the enzyme myosin light-chain phosphatase, leading to the dephosphorylation of myosin and muscle relaxation. This delicate balance is crucial for proper muscle function.
Neuronal Signalling and Synaptic Plasticity:
In neurons, calmodulin is essential for neurotransmitter release and synaptic plasticity. It modulates the activity of proteins involved in vesicle fusion and neurotransmitter release. Additionally, calmodulin-dependent protein kinases (CaMKs) are critical for synaptic plasticity, learning, and memory. The intricate interplay between calmodulin and neuronal proteins underpins the fundamental processes of learning and cognition.
Implications in Disease and Therapeutics:
Dysregulation of calmodulin has been implicated in various diseases, including cardiac arrhythmias and neurodegenerative disorders. Mutations in calmodulin genes can lead to aberrant calcium signalling and cellular dysfunction. Consequently, understanding these molecular mechanisms offers potential therapeutic targets. Researchers are exploring calmodulin inhibitors and modulators for conditions like cardiac arrhythmias, aiming to restore normal cellular function.
Conclusion:
Calmodulin, with its remarkable structural versatility and central role in cellular signalling, epitomizes the complexity of biological regulation. Its influence spans from the fundamental processes of muscle contraction to the intricacies of neuronal signalling. Unravelling the mysteries of calmodulin not only deepens our understanding of basic biological phenomena but also holds the promise of innovative therapeutic interventions. This research illuminates calmodulin's significance, emphasizing its position as a master regulator in the orchestra of cellular life.
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 :
HSV-1 gDDescription:
Herpes Simplex Virus-1 gD Recombinant
Product # :
HSV-221Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- formulation
- purity
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Description
The E.Coli derived recombinant protein contains the HSV-1 gD immunodominant regions, 266-394 amino acids and fused to a GST-Tag at C-terminus.
Formulation
25mM Tris-HCl pH 8, 1mM EDTA, and 50% glycerol.
Purity
HSV-1 gD protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
Entry of HSV into the host cell involves interactions of several viral glycoproteins with cell surface receptors. The virus particle is covered by an envelope which, when bound to specific receptors on the cell surface, will fuse with the cell membrane and create an opening, or pore, through which the virus enters the host cell. The sequential stages of HSV entry are analagous to those of other viruses. At first, complementary receptors on the virus and cell surface bring the two membranes into proximity. In an intermediate state, the two membranes begin to merge, forming a hemifusion state. Finally, a stable entry pore is formed through which the viral envelope contents are introduced to the host cell.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
HSV-1 gD protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Specificity
Immunoreactive with sera of HSV-infected individuals.
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Purification Method
HSV-1 gD was purified by proprietary chromatographic technique.
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 :
IGF1 Human, R36QDescription:
Insulin Like Growth Factor-1, Mutant R36Q Human Recombinant
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Product # :
CYT-1090Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
IGF1 R36Q Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7kDa. The IGF1 R36Q is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IGF1 R36Q Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM PB and 150 mM NaCl, pH 5.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
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Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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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Solubility
It is recommended to reconstitute the lyophilized IGF1 R36Q 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
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSQRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
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 :
MAT2A AntibodyDescription:
Methionine Adenosyltransferase II Alpha, Mouse Anti Human
MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.
Product # :
ANT-388Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
MAT2A is an important enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP. MAT2A is expressed in extrahepatic tissues. In liver, MAT2A expression associates with growth, dedifferentiation, and cancer. NF-kappa B and AP-1 are necessary for basal MAT2A expression in HepG2 cells and mediate the increase in MAT2A expression in response to TNF-alpha. Up-regulation of MAT2A provides growth improvement and s-adenosylmethionine and methylthioadenosine thus can block mitogenic signaling in colon cancer cells. Lower expression of both MAT2A and MAT2beta and interfere with leptin signaling in liver cancer cells.
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Synonyms
MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.
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Immunogen
Anti-human MAT2A mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human MAT2A amino acids 1-395 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
PAT3A2AT.
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Applications
MAT2A antibody has been tested by ELISA, Western blot and immunohistochemistry 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 is 1:1,000 ~ 1:2,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:1,000 and Immunohistochemistry is 1:50.
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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
MAT2A 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.
- View Data Sheet
Name :
Avidin ProteinDescription:
Avidin
Avidin, AVD, AVID.
Product # :
PRO-500Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- biological activity
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Description
Avidin is a glycosylated polypeptide chain having a molecular mass of 68kDa and containing 4 subunits each with a binding site for biotin. The Avidin is purified by affinity chromatographic techniques.The purification procedure ensures minimal contamination by other proteins or DNA.The resulting high activity and purity of the product gives very low non-specific binding (NSB).
Source
Hen's egg white.
Biological Activity
15.0 units/mg protein, 1 unit binds 1µg biotin.
More Info
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Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) each of which can bind to biotin with a high degree of affinity and specificity. Avidin molecular weight in its tetrameric form is estimated to be between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of four to five mannose and three N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.
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Synonyms
Avidin, AVD, AVID.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Avidin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
VZV ORF26Description:
Varicella Zoster Virus ORF26 Recombinant
Product # :
VZV-233Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
The E.Coli derived recombinant protein contains the VZV ORF26 immunodominant regions, amino acids 9-33, 184-208.
Source
Escherichia Coli.
Formulation
25mM Tris-Hcl pH 7.2, 1mM EDTA and 50% glycerol.
Purity
Varicella protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
VZV is closely related to the herpes simplex viruses(HSV), sharing much genomehomology. The known envelope glycoproteins (gB, gC, gE, gH, gI, gK, gL) correspond with those in HSV, however there is no equivalent of HSV gD. VZV virons are spherical and 150-200 nm in diameter. Their lipidenvelope encloses the nucleocapsid of 162 capsomeres arranged in a hexagonalform. Its DNAis a single, linear, double-stranded molecule, 125,000 nt long. The virus is very susceptible to disinfectants, notably sodium hypochlorite. Within the body it can be treated by a number of drugs and therapeutic agents including aciclovir, zoster-immune globulin(ZIG), and vidarabine.
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Stability
Varicella protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Specificity
Immunoreactive with sera of VZV-infected individuals.
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Purification Method
Varicella was purified by proprietary chromatographic technique.
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 :
TINAGL1 HumanDescription:
Tubulointerstitial Nephritis Antigen Like 1 Human Recombinant
Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.
Product # :
PRO-1675Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
800x600 TINAGL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 469 amino acids (22-467) and having a molecular mass of 52.5 kDa.TINAGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TINAGL1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Tubulointerstitial Nephritis Antigen Like 1 also known as TINAGL1 is similar in sequence to tubulointerstitial nephritis antigen, a secreted glycoprotein which is identified by antibodies in several types of immune-related tubulointerstitial nephritis. Three transcript variants encoding different isoforms are known for TINAGL1.
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Synonyms
Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.
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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 MGSAQQGRGR RELAPGLHLR GIRDAGGRYC QEQDLCCRGR ADDCALPYLG AICYCDLFCN RTVSDCCPDF WDFCLGVPPP FPPIQGCMHG GRIYPVLGTY WDNCNRCTCQ ENRQWQCDQE PCLVDPDMIK AINQGNYGWQ AGNHSAFWGM TLDEGIRYRL GTIRPSSSVM NMHEIYTVLN PGEVLPTAFE ASEKWPNLIH EPLDQGNCAG SWAFSTAAVA SDRVSIHSLG HMTPVLSPQN LLSCDTHQQQ GCRGGRLDGA WWFLRRRGVV SDHCYPFSGR ERDEAGPAPP CMMHSRAMGR GKRQATAHCP NSYVNNNDIY QVTPVYRLGS NDKEIMKELM ENGPVQALME VHEDFFLYKG GIYSHTPVSL GRPERYRRHG THSVKITGWG EETLPDGRTL KYWTAANSWG PAWGERGHFR IVRGVNECDI ESFVLGVWGR VGMEDMGHH.
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.