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Name :
Myoglobin HumanDescription:
Myoglobin Human Recombinant
Myoglobin, MB, PVALB, MGC13548.
Product # :
PRO-336Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Myoglobin Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 17.67 kDa. The Myoglobin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile solution contains phosphate-buffered saline (pH 7.4) and 0.05% NaN3.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. It is a haemoprotein that contributs to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobin’s molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is uninfluenced by the oxygen pressure in the surrounding tissue. Myoglobin is frequently referred to as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. Myoglobin is responsible for the pigments that make meat red. The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. Myoglobin is found in Type I muscle, Type II A and Type II B, but it is mostly deemed that myoglobin is not found in smooth muscle. Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. Even though the released myoglobin is filtered by the kidneys, it is toxic to the renal tubular epithelium and thus may cause acute renal failure.
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Synonyms
Myoglobin, MB, PVALB, MGC13548.
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Physical Appearance
Sterile Filtered brownish solution.
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Stability
Myoglobin should be stored at 4°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please do not freeze.
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 :
DsbADescription:
Disulfide Oxidoreductase Recombinant
DsbA, Thiol:disulfide interchange protein dsbA.
Product # :
ENZ-276Price :
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Shipped at Room temp
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Description
Disulfide Oxidoreductase produced in E.Coli is a periplasmic protein isolated from E. coli, containing 208 amino acids having a molecular mass of 23,149 Dalton. The DsbA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized after from a sterile solution containing 50mM sodium phosphate buffer and 100mM sodium chloride.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
DsbA appears to be necessary for correct formulation of disulfide bonds in exported proteins in vivo. DsbA is useful as a standard in immunoblotting. This protein catalyses the reduction and exchange of disulfide bonds and the oxidation of free sulfhydryl groups in vitro. It is the strongest oxidant of the thioredoxin superfamily. This thio/disulfide oxidoreductase is required for efficient disulfide bond formation in the periplasm of E. coli.
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Synonyms
DsbA, Thiol:disulfide interchange protein dsbA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized DsbA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DsbA 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 DsbA 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
MKKIWLALAGLVLAFSASAAQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQLNPQGMDTSNMDVFVQQYADTVKYLSEKK
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 :
IL11RA RatDescription:
Interleukin 11 Receptor Subunit Alpha Rat Recombinant
Interleukin-11 receptor subunit alpha, IL-11 receptor subunit alpha, IL-11R subunit alpha, IL-11R-alpha, IL-11RA, Il11ra1.
Product # :
CYT-990Price :
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Description
Interleukin 11 Receptor Subunit Alpha Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (24-371a.a.) and having a molecular mass of 39.2kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL11RA is fused with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL11RA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
Interleukin 11 Receptor Subunit Alpha (IL11RA) which belongs to the hematopoietic cytokine receptor family is a receptor for interleukin-11. Interleukin 11 is a stromal cell-derived cytokine which is a member of a family of pleiotropic and redundant cytokines that employ the gp130 transducing subunit in their high affinity receptors. This specific receptor is quite similar to ciliary neurotrophic factor, since both contain an extracellular region with a two-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 are able to utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex is involved in the control of proliferation and/or differentiation of skeletogenic progenitor or additional mesenchymal cells.
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Synonyms
Interleukin-11 receptor subunit alpha, IL-11 receptor subunit alpha, IL-11R subunit alpha, IL-11R-alpha, IL-11RA, Il11ra1.
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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
TPCPQAWGPP GVQYGQPGRP VMLCCPGVNA GTPVSWFRDG DSRLLQGPDS GLGHRLVLAQ VDSRDEGTYV CRTLDGVFGG MVTLKLGSPP ARPEVSCQAV DYENFSCTWS PGRVSGLPTR YLTSYRKKTL PGAESQRESP STGPWPCPQD PLEASRCVVH GAEFWSEYRI NVTEVNPLGA STCLLDVRLQ RILRPDPPQG LRVESVPGYP RRLHASWTYP ASWRRQPHFL LKFRLQYRPA QHPAWSTVEP IGLEELITDA VAGLPHAVRV SARDFLDAGT WSAWSPEAWG TPSTGPLRDE VPDGSRGHEQ KLEAAAQEDS PAPPSPSLQP DPRPLDHRDP LEQVAVLAVE HHHHHH.
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Background
What is the molecular weight/Mw of IL11RA RAT Protein?
IL11RA RAT Protein has a total Mw of 39.2kDa.
What is the source or expression system of IL11RA RAT Protein?
Sf9, Baculovirus cells.
What is the Purity of IL11RA RAT Protein?
IL11RA RAT Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of IL11RA RAT Protein?
The biological functionality of IL11RA RAT Protein will be determined in the future.
What is the amino acid sequence of IL11RA RAT Protein?
TPCPQAWGPP GVQYGQPGRP VMLCCPGVNA GTPVSWFRDG DSRLLQGPDS GLGHRLVLAQ VDSRDEGTYV CRTLDGVFGG MVTLKLGSPP ARPEVSCQAV DYENFSCTWS PGRVSGLPTR YLTSYRKKTL PGAESQRESP STGPWPCPQD PLEASRCVVH GAEFWSEYRI NVTEVNPLGA STCLLDVRLQ RILRPDPPQG LRVESVPGYP RRLHASWTYP ASWRRQPHFL LKFRLQYRPA QHPAWSTVEP IGLEELITDA VAGLPHAVRV SARDFLDAGT WSAWSPEAWG TPSTGPLRDE VPDGSRGHEQ KLEAAAQEDS PAPPSPSLQP DPRPLDHRDP LEQVAVLAVE HHHHHH.
What applications can IL11RA RAT Protein be used in?
IL11RA RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL11RA RAT Protein?
The endotoxin level is minimal, IL11RA RAT Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL11RA RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL11RA RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PIP HumanDescription:
Prolactin-Induced Protein Human
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, PIP, GCDFP15, GPIP4.
Product # :
CYT-779Price :
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Shipping Method :
Shipped at Room temp
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Description
The Prolactin-Induced Protein produced from Human Seminal Plasma has a molecular mass of 13.52kDa (calculated without glycosylation) containing 118 amino acid residues.
Source
Human Seminal Plasma.
Formulation
PIP protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prolactin inducible protein (PIP) is a 17kDa glycoprotein existing in human seminal plasma. PIP is synthesized as a 146 amino acid long polypeptide exhibiting high sequence similarity with mouse submaxillary gland with a single glycosylation site. The precise biological functions of PIP are still ambiguous but various functions have been assigned to PIP due its existence at high concentration in biological fluids. PIP binds to various proteins such as fibrinogen, actin, keratin, myosin and tropomyosin. PIP is also expressed in pathological conditions of the mammary gland and in some exocrine tissues, such as the lacrimal, salivary and sweat glands. Due to PIP’s association with secretory cell differentiation, it has been used in diagnostic evaluation of tumors of breast, salivary gland, and skin.
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Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, PIP, GCDFP15, GPIP4.
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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 0.5 mg/ml and let the lyophilized pellet dissolve completely. PIP 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
QDNTRKIIIK NFDIPKSVRP NDEVTAVLAV QTELKECMVV KTYLISSIPL QGAFNYKYTA CLCDDNPKTF YWDFYTNRTV QIAAVVDVIR ELGICPDDAA VIPIKNNRFY TIEILKVE.
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Human Virus Test
Samples from each donor have been tested and found negative for HBsAg, HIV1+2, HCV, syphilis, aHBc, RRR.
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 :
GP1BB HumanDescription:
Glycoprotein Ib Platelet Subunit Beta Human Recombinant
GPIBB, glycoprotein Ib platelet subunit beta, BDPLT1,GP-Ib beta, BS, CD42C ,GPIbbeta, Antigen CD42b-beta, GPIb-beta, GPIbB, Platelet glycoprotein Ib beta chain.
Product # :
PRO-2774Price :
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Shipped with Ice Packs
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Description
GP1BB Human Recombinant is a single, glycosylated, polypeptide chain (26-147 a.a) containing a total of 131 amino acids, having a molecular mass of 14.0 kDa. GP1BB is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The GP1BB solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
GPIBB, glycoprotein Ib platelet subunit beta, BDPLT1,GP-Ib beta, BS, CD42C ,GPIbbeta, Antigen CD42b-beta, GPIb-beta, GPIbB, Platelet glycoprotein Ib beta chain.
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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
DGSCPAPCSC AGTLVDCGRR GLTWASLPTA FPVDTTELVL TGNNLTALPP GLLDALPALR TAHLGANPWR CDCRLVPLRA WLAGRPERAP YRDLRCVAPP ALRGRLLPYL AEDELRAACA PGPLCHHHHH H.
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Background
Glycoprotein 1b beta (GP1BB) is a crucial component of the platelet glycoprotein Ib-IX-V complex, playing a pivotal role in platelet function and hemostasis. This research aims to explore the structure, function, and implications of GP1BB protein in platelet adhesion, aggregation, and the development of thrombotic disorders. Understanding the molecular mechanisms and regulatory roles of GP1BB can provide valuable insights into its potential as a therapeutic target for thrombotic diseases.
Structure and Expression of GP1BB Protein:
GP1BB is a transmembrane protein consisting of an extracellular domain, a single transmembrane region, and a short cytoplasmic tail. It is predominantly expressed on the surface of platelets, where it interacts with von Willebrand factor (VWF) and other components of the glycoprotein Ib-IX-V complex. GP1BB is crucial for mediating platelet adhesion to damaged endothelium and the formation of stable platelet aggregates at the site of injury.
GP1BB and Platelet Adhesion:
GP1BB interacts with VWF, which is exposed upon vascular injury. This interaction facilitates the initial attachment of platelets to the damaged endothelium. GP1BB also participates in the formation of high-affinity bonds between platelets and VWF, contributing to the stabilization of platelet adhesion and the initiation of platelet aggregation. Dysregulation of GP1BB-mediated platelet adhesion can lead to abnormal clot formation and thrombotic disorders.
Implications of GP1BB in Thrombotic Disorders:
Defects or mutations in the GP1BB gene can result in Bernard-Soulier syndrome (BSS), a rare inherited bleeding disorder characterized by giant platelets, thrombocytopenia, and impaired platelet adhesion. BSS patients often experience excessive bleeding and bruising due to defective GP1BB function. On the other hand, abnormal activation or overexpression of GP1BB has been associated with increased risk of thrombotic events, such as myocardial infarction and stroke.
Therapeutic Strategies Targeting GP1BB:
Given its crucial role in platelet function and thrombotic disorders, GP1BB represents a potential target for therapeutic interventions. Strategies aimed at modulating GP1BB expression or function have been explored. This includes the development of monoclonal antibodies or small molecule inhibitors that selectively target GP1BB and interfere with its interaction with VWF or other binding partners. Such approaches aim to prevent excessive platelet adhesion and aggregation, reducing the risk of thrombotic events.
Challenges and Future Directions:
While targeting GP1BB shows promise, several challenges need to be addressed. The development of specific inhibitors or modulators of GP1BB that do not interfere with its physiological functions is crucial. Additionally, understanding the complex interplay between GP1BB and other platelet receptors and signaling pathways is essential for the development of effective therapeutic strategies.
Conclusion:
The study of GP1BB protein provides valuable insights into its central role in platelet adhesion, aggregation, and thrombotic disorders. Understanding the molecular mechanisms and functional implications of GP1BB opens avenues for the development of targeted therapies for thrombotic diseases. Further research on GP1BB protein, its interactions, and its modulation in pathological conditions will contribute to the development of novel therapeutic interventions to mitigate the risk of thrombotic events and improve patient outcomes.
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 :
USP46 HumanDescription:
Ubiquitin Specific Peptidase 46 Human Recombinant
Ubiquitin carboxyl-terminal hydrolase 46, Deubiquitinating enzyme 46, Ubiquitin thioesterase 46, Ubiquitin-specific-processing protease 46, USP46.
Product # :
PRO-1866Price :
Quantity :
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Shipped with Ice Packs
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Description
USP46 Human Recombinant produced in E. coli is. a single polypeptide chain containing 389 amino acids (1-366) and having a molecular mass of 44.8kDa. USP46 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The USP46 solution (0.25mg/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.
Citations
More Info
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Introduction
USP46 is a part of a large family of cysteine proteases that function as deubiquitinating enzymes which interacts with WDR48 to have a high activity. USP46 operates by mediating the deubiquitination of GAD1/GAD67.
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Synonyms
Ubiquitin carboxyl-terminal hydrolase 46, Deubiquitinating enzyme 46, Ubiquitin thioesterase 46, Ubiquitin-specific-processing protease 46, USP46.
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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 MGSMTVRNIA SICNMGTNAS ALEKDIGPEQ FPINEHYFGL VNFGNTCYCN SVLQALYFCR PFRENVLAYK AQQKKKENLL TCLADLFHSI ATQKKKVGVI PPKKFISRLR KENDLFDNYM QQDAHEFLNY LLNTIADILQ EEKKQEKQNG KLKNGNMNEP AENNKPELTW VHEIFQGTLT NETRCLNCET VSSKDEDFLD LSVDVEQNTS ITHCLRDFSN TETLCSEQKY YCETCCSKQE AQKRMRVKKL PMILALHLKR FKYMEQLHRY TKLSYRVVFP LELRLFNTSS DAVNLDRMYD LVAVVVHCGS GPNRGHYITI VKSHGFWLLF DDDIVEKIDA QAIEEFYGLT SDISKNSESG YILFYQSRE.
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 :
LYVE1 Human 25-235 a.a.Description:
Lymphatic Vessel Endothelial Hyaluronic Acid Receptor 1 (25-235 a.a) Human Recombinant
HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing protein.
Product # :
PKA-349Price :
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Description
LYVE1 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 229 amino acids and having a molecular mass of 24.8 kDa. As a result of glycosylation, the LYVE1 migrates on SDS-PAGE at approximately 50 kDa. LYVE1 is expressed with 15 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
High Five insect cells.
Formulation
The LYVE1 protein solution contains 20mM Tris buffer pH-7.5 and 10% Glycerol.
Purity
Greater than 90.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Citations
More Info
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Introduction
LYVE1 is a selective marker of the lymphatic endothelium & a surface endocytic receptor for both soluble and immobilized hyaluronan, LYVE1 is an extracellular glycosaminoglycan that plays a role in cell adhesion and migration. LYVE1 functions in lympathic hyaluronan transport and is involved in tumor metastasis. Recombinant human LYVE1 was expressed in and purified by conventional chromatography techniques. The normal adult human choroid is endowed with a significant number of LYVE-1 positive macrophages. LYVE-1 is expressed in a reticulum cell neoplasm in an axillary lymph node. This reticulum cell sarcoma is a lymphatic sinus lining cell sarcoma which might represent another subtype of reticulum cell sarcomas.
LYVE-1 immunohistochemistry is a functional method for detecting lymphatics invaded by cancer cells, and detailed examination of the submucosa around the tumor is important for predicting LN metastasis. -
Synonyms
HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing protein.
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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
DPLRAEELS IQVSCRIMGI TLVSKKANQQ LNFTEAKEAC RLLGLSLAGK DQVETALKAS FETCSYGWVG DGFVVISRIS PNPKCGKNGV GVLIRKVPVS RQFAAYCYNS SDTWTNSCIP EIITTKDPIF NTQTATQTTE FIVSDSTYSV ASPYSTIPAP TTTPPAPAST SIPRRKKLIC VTEVFMETST MSTETEPFVE NKAAFKNEAA GFGGSGRLVP RGSHHHHHH.
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 :
CRP Human RecombinantDescription:
c-Reactive Protein Human Recombinant
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
Product # :
PRO-335Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human CRP produced in E.Coli is a non-glycosylated polypeptide chain having a total molecular mass of 115 kDa that corresponds to the pentamer structure of 23 kDa monomer determined by amino acid sequence. The CRP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile protein solution contains 20mM Tris (pH 7.5), 2mM CaCl2, 0.14M NaCl and 0.05% NaN3.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.
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Synonyms
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
CRP should be stored at all times at 4°C.
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 :
OX40L HumanDescription:
OX40 Ligand Human Recombinant
Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.
Product # :
CYT-1226Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OX40L Human Recombinant is a single, glycosylated, polypeptide chain (51-183 a.a) containing a total of139 amino acids and having a molecular mass of 16.2 kDa. OX40L is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human OX40/TNFRSF4.
Citations
More Info
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Synonyms
Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.
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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
QVSHRYPRIQ SIKVQFTEYK KEKGFILTSQ KEDEIMKVQN NSVIINCDGF YLISLKGYFS QEVNISLHYQ KDEEPLFQLK KVRSVNSLMV ASLTYKDKVY LNVTTDNTSL DDFHVNGGEL ILIHQNPGEF CVLHHHHHH.
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Background
OX40 Ligand (OX40L), a member of the tumor necrosis factor (TNF) superfamily, plays a pivotal role in regulating immune responses and orchestrating the delicate balance between activation and tolerance. The human recombinant form of OX40L has emerged as a potent tool in immunology, offering insights into its molecular intricacies and potential applications in therapeutic interventions. This research embarks on a journey to unravel the multifaceted role of OX40L Human Recombinant, shedding light on its structural attributes, signaling pathways, and its promising avenues in immunotherapy. By delving into the properties of OX40L, scientists aim to expand our understanding of immune modulation and open new frontiers in the treatment of immune-related disorders.
Structural Insights into OX40L Human Recombinant:
OX40L, as a trimeric transmembrane protein, exhibits a unique structural configuration that governs its interactions with the OX40 receptor on T cells. The human recombinant form, engineered for controlled study, provides a window into the three-dimensional intricacies of the ligand. Understanding its structure is pivotal for deciphering how OX40L engages with its receptor and modulates immune responses.
Immunomodulatory Signaling Pathways:
OX40L binding to its cognate receptor OX40 on T cells triggers intricate signaling cascades that impact immune cell activation, proliferation, and cytokine production. The OX40-OX40L axis is a crucial regulator of T cell function, influencing both effector and regulatory T cell responses. Unraveling the specific pathways activated by OX40L Human Recombinant provides valuable insights into the modulation of immune responses in health and disease.
Applications in Immunotherapy:
The immunomodulatory properties of OX40L make it an attractive candidate for therapeutic interventions. OX40L Human Recombinant, in preclinical and clinical studies, is being explored for its potential in enhancing antitumor immune responses. By harnessing the ligand's ability to stimulate effector T cells and memory T cell formation, researchers aim to develop novel immunotherapies for cancer and other immune-related disorders.
OX40L in Autoimmune Diseases:
Conversely, OX40L's role in autoimmune diseases has spurred investigations into its inhibition as a therapeutic strategy. Blocking the OX40-OX40L interaction has shown promise in mitigating autoimmune responses, presenting a potential avenue for the development of treatments for conditions such as rheumatoid arthritis and inflammatory bowel disease.
While the potential of OX40L Human Recombinant in immunotherapy is promising, challenges persist. Fine-tuning its applications, understanding potential side effects, and optimizing dosages are critical considerations for translational success. Additionally, comprehending the context-dependent nature of OX40L signaling is essential for tailoring therapeutic strategies to specific diseases and patient profiles.
OX40L Human Recombinant stands at the forefront of immunomodulation research, offering a lens through which we can unravel the complexities of immune responses. Its structural insights, signaling pathways, and therapeutic applications position it as a key player in the evolving landscape of immunotherapy. As researchers continue to dissect the molecular nuances of OX40L, they not only expand our understanding of immune regulation but also pave the way for transformative advancements in the treatment of cancer and autoimmune diseases, shaping the future of precision medicine and immunotherapy.
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 :
Heparin Sodium PorcineDescription:
Heparin Sodium Porcine
Heparin, Porcine Heparin, Heparin Pig.
Product # :
PRO-2811Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- biological activity
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Description
Heparin Sodium Porcine is a natural native protein.
Source
Porcine Mucosa.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Biological Activity
200IU/mg.
Citations
More Info
-
Synonyms
Heparin, Porcine Heparin, Heparin Pig.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Heparin Sodium Porcine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heparin Sodium Porcine should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Heparin Sodium Porcine in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
Heparin sodium, a highly sulfated glycosaminoglycan, has long been recognized for its pivotal role as an anticoagulant. In porcine systems, the study of Heparin Sodium takes on significance not only for its therapeutic applications in veterinary medicine but also for its potential translational impact on human health. This research embarks on an exploration of Heparin Sodium in porcine contexts, unraveling its structural intricacies, pharmacological attributes, and broader implications for health and biomedical interventions. By delving into the properties of Heparin Sodium in porcine models, scientists aim to deepen our understanding of its anticoagulant mechanisms, therapeutic potential, and the potential avenues for cross-species applications in healthcare.
Structural Insights into Porcine Heparin Sodium:
Porcine-derived Heparin Sodium, similar to its counterparts in other species, possesses a complex and highly sulfated structure. Understanding the nuances of its structure is fundamental for deciphering how Heparin Sodium interacts with antithrombin, leading to the inhibition of clotting factors and preventing the formation of blood clots. Structural insights contribute to optimizing its therapeutic efficacy.
Pharmacological Attributes and Anticoagulant Mechanisms:
Heparin Sodium's pharmacological attributes are central to its anticoagulant effects. In porcine systems, Heparin Sodium acts as an indirect anticoagulant by accelerating the activity of antithrombin, a natural inhibitor of clotting factors. Elucidating the specific mechanisms by which porcine Heparin Sodium modulates coagulation pathways contributes to refining its dosage and application in veterinary medicine.
Therapeutic Potential in Veterinary Medicine:
Porcine Heparin Sodium holds significant therapeutic potential in veterinary medicine, where clotting disorders and thrombotic events are prevalent. Understanding its pharmacokinetics, dosage requirements, and potential interactions with other drugs is crucial for optimizing its use in porcine healthcare. Additionally, exploring its safety profile in porcine models contributes to ensuring the well-being of animals under treatment.
Cross-Species Applications and Translational Insights:
Beyond its veterinary applications, porcine Heparin Sodium provides insights into potential cross-species applications, particularly in translational medicine. Understanding the similarities and differences in its anticoagulant mechanisms between porcine and human systems may open avenues for therapeutic innovations with relevance to both animal and human health.
Challenges and Future Directions:
While porcine Heparin Sodium presents opportunities for advancements in veterinary medicine and translational research, challenges persist. Fine-tuning its applications, addressing potential variations in its anticoagulant properties across different porcine breeds, and ensuring its safety and efficacy in diverse clinical scenarios are critical considerations for translational success.
Porcine Heparin Sodium emerges as a key player in the landscape of anticoagulation, offering a bridge between veterinary and translational medicine. Its structural insights, pharmacological attributes, and therapeutic potential in porcine systems contribute not only to veterinary care but also offer translational insights with implications for human health. As researchers continue to unravel the molecular intricacies of porcine Heparin Sodium, they not only deepen our understanding of anticoagulation in veterinary contexts but also pave the way for innovative biomedical applications, shaping the future of healthcare for both animals and humans.
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 :
Cytochrome-C BovineDescription:
Cytochrome-C Bovine
CYCS, CYC, cyt c
Product # :
PRO-2810Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
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Description
Cytochrome-C Bovine is a natural native protein.
Source
Bovine.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 99.0%.
Citations
More Info
-
Synonyms
CYCS, CYC, cyt c
-
Physical Appearance
Reddish or dark brown crystalline powder.
-
Stability
Lyophilized Cytochrome-C Bovine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cytochrome-C Bovine should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Cytochrome-C Bovine in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
Bovine Cytochrome c in Health and Disease:
Understanding the behavior of Cytochrome c in bovine systems has implications for veterinary medicine and livestock health. Alterations in mitochondrial function, reflected in changes in Cytochrome c dynamics, may be indicative of metabolic disorders, oxidative stress, or other pathological conditions. Bovine Cytochrome c studies contribute to our knowledge of mitochondrial dysfunction in diseases affecting cattle, potentially paving the way for diagnostic and therapeutic strategies.
Challenges and Future Directions:
While the study of Cytochrome c in bovine systems provides a wealth of insights, challenges persist. Fine-tuning experimental methodologies, exploring the interplay with other mitochondrial components, and deciphering the specificities in bovine systems are critical considerations for advancing our understanding. Additionally, linking changes in Cytochrome c behavior to specific physiological outcomes in cattle poses a challenge, requiring comprehensive investigations in diverse contexts.
Bovine Cytochrome c emerges as a sentinel player in the intricate dance of cellular respiration, offering a window into the energetic dynamics of bovine mitochondria. Its structural insights, functional significance, and implications in health and disease position it as a central focus in understanding cellular bioenergetics in cattle. As researchers continue to unravel the molecular intricacies of bovine Cytochrome c, they not only deepen our understanding of mitochondrial function but also contribute to advancements in veterinary medicine and the optimization of livestock health, shaping the future of sustainable and healthy cattle farming practices.
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 :
CRTAP HumanDescription:
Cartilage Associated Protein Human Recombinant
CASP, LEPREL3, OI7, Cartilage-associated protein, CRTAP.
Product # :
PRO-1862Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
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Description
CRTAP Human Recombinant produced in E. coli is. a single polypeptide chain containing 398 amino acids (27-401) and having a molecular mass of 46.4kDa. CRTAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRTAP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Cartilage-associated protein (CRTAP) is a secreted protein localizing to the extracellular space which takes part in collagen post-translational modifications, extracellular fibril assembly and intracellular trafficking. CRTAP which is mainly expressed with predominant expression in articular chondrocytes is essential for efficient 3-hydroxylation of fibrillar collagen prolyl residues. Mutations in the gene encoding CRTAP might cause to autosomal recessive osteogenesis imperfecta (OI) type 7 and type 2B.
-
Synonyms
CASP, LEPREL3, OI7, Cartilage-associated protein, CRTAP.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQYERYSF RSFPRDELMP LESAYRHALD KYSGEHWAES VGYLEISLRL HRLLRDSEAF CHRNCSAAPQ PEPAAGLASY PELRLFGGLL RRAHCLKRCK QGLPAFRQSQ PSREVLADFQ RREPYKFLQF AYFKANNLPK AIAAAHTFLL KHPDDEMMKR NMAYYKSLPG AEDYIKDLET KSYESLFIRA VRAYNGENWR TSITDMELAL PDFFKAFYEC LAACEGSREI KDFKDFYLSI ADHYVEVLEC KIQCEENLTP VIGGYPVEKF VATMYHYLQF AYYKLNDLKN AAPCAVSYLL FDQNDKVMQQ NLVYYQYHRD TWGLSDEHFQ PRPEAVQFFN VTTLQKELYD FAKENIMDDD EGEVVEYVDD LLELEETS.
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 :
HDGFL1 HumanDescription:
Hepatoma Derived Growth Factor-Like 1 Human Recombinant
Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.
Product # :
CYT-850Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
- purity
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Description
HDGFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-251 a.a) and having a molecular mass of 29.6kDa.HDGFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HDGFL1 protein solution (0.25mg/ml) containing Phosphate buffered saline, (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Hepatoma Derived Growth Factor-Like 1 (HDGFL1) is a member of the HDGF family and contains 1 PWWP domain.
-
Synonyms
Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.
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Background
What is the molecular weight/Mw of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein has a total Mw of 29.6kDa.
What is the source or expression system of HDGFL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of HDGFL1 HUMAN Protein?
The biological functionality of HDGFL1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of HDGFL1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.
What applications can HDGFL1 HUMAN Protein be used in?
HDGFL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HDGFL1 HUMAN Protein?
The endotoxin level is minimal, HDGFL1 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
AIDA HumanDescription:
Axin Interactor Dorsalization Associated Human Recombinant
C1orf80, RP11-378J18.7, Axin interactor, dorsalization-associated protein, Axin interaction partner and dorsalization antagonist, AIDA.
Product # :
PRO-1370Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
- purity
- More Info
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Description
AIDA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-306 a.a) and having a molecular mass of 37.4kDa. AIDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
AIDA protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.2M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Axin interactor, dorsalization-associated (AIDA) operates as a ventralizing factor during embryogenesis. AIDA inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. That in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling.
-
Synonyms
C1orf80, RP11-378J18.7, Axin interactor, dorsalization-associated protein, Axin interaction partner and dorsalization antagonist, AIDA.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEVTRS LLQRWGASFR RGADFDSWGQ LVEAIDEYQI LARHLQKEAQ AQHNNSEFTE EQKKTIGKIA TCLELRSAAL QSTQSQEEFK LEDLKKLEPI LKNILTYNKE FPFDVQPVPL RRILAPGEEE NLEFEEDEEE GGAGAGSPDS FPARVPGTLL PRLPSEPGMT LLTIRIEKIG LKDAGQCIDP YITVSVKDLN GIDLTPVQDT PVASRKEDTY VHFNVDIELQ KHVEKLTKGA AIFFEFKHYK PKKRFTSTKC FAFMEMDEIK PGPIVIELYK KPTDFKRKKL QLLTKKPLYL HLHQTLHKE.
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 :
ANXA2 HumanDescription:
Annexin A2 Human
ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.
Product # :
PRO-1573Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
The Human Annexin A2 produced from Human Adipose Tissue has a molecular mass of 38.472kDa (calculated without glycosylation) containing 338 amino acid residues.
Source
Human Adipose Tissue.
Formulation
ANXA2 protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl and pH 6.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
ANXA2 is part of the annexin family and is involved in the regulation of cellular growth and in signal transduction pathways. ANXA2 protein functions as an autocrine factor which increases osteoclast formation and bone resorption. ANXA2 is associated with sickle cell osteonecrosis. Reduced ANXA2 expression is associated with osteosarcoma metastases. ANXA2 is part of the putative cell surface vitamin D binding protein binding site complex and functions to mediate the chemotactic cofactor effect. ANXA2 is involved in dysferlin deficiency and in muscular dystrophies. Human colon adenocarcinoma cell differentiation is related with an up-regulation of ANXA2.
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Synonyms
ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
STVHEILCKL SLEGDHSTPP SAYGSVKAYT NFDAERDALN IETAIKTKGV DEVTIVNILT NRSNAQRQDI AFAYQRRTKK ELASALKSAL SGHLETVILG LLKTPAQYDA SELKASMKGL GTDEDSLIEI ICSRTNQELQ EINRVYKEMY KTDLEKDIIS DTSGDFRKLM VALAKGRRAE DGSVIDYELI DQDARDLYDA GVKRKGTDVP KWISIMTERS VPHLQKVFDR YKSYSPYDML ESIRKEVKGD LENAFLNLVQ CIQNKPLYFA DRLYDSMKGK GTRDKVLIRI MVSRSEVDML KIRSEFKRKY GKSLYYYIQQ DTKGDYQKAL LYLCGGDD.
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 :
TFAM HumanDescription:
Transcription Factor-A Recombinant Human
Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.
Product # :
PRO-095Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TFAM produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (43-246.a.a) and having a molecular mass of 26.6kDa. TFAM is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TFAM protein solution (0.25mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TFAM is a mitochondrial transcription factor which is a main activator of mitochondrial transcription and is also a participant in mitochondrial genome replication. TFAM is situated primarily in the nuclei of elongated spermatids and takes part in the regulation of gene expression of the haploid male genome. TFAM is linked to mitochondrial disorder in humans characterized by ocular myopathy, exercise intolerance and muscle wasting.
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Synonyms
Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSVLASCPK KPVSSYLRFS KEQLPIFKAQ NPDAKTTELI RRIAQRWREL PDSKKKIYQD AYRAEWQVYK EEISRFKEQL TPSQIMSLEK EIMDKHLKRK AMTKKKELTL LGKPKRPRSA YNVYVAERFQ EAKGDSPQEK LKTVKENWKN LSDSEKELYI QHAKEDETRY HNEMKSWEEQ MIEVGRKDLL RRTIKKQRKY GAEEC
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 :
GKN1 HumanDescription:
Gastrokine 1 Human Recombinant
BRICHOS domain containing 1, 18 kDa antrum mucosa protein, gastrokine 1, Protein CA11, AMP-18, BRICD1, foveolin, FOV.
Product # :
PRO-1206Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GKN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 223 amino acids (1-199) and having a molecular mass of 24.5 kDa.GKN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GKN1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Gastrokine-1 (GKN1) is a member of the gastrokine family. GKN1 has mitogenic activity and is involved in preserving the integrity of the gastric mucosal epithelium. GKN1 is down-regulated in human gastric cancer tissue in comparison to normal gastric mucosa. GKN1 is expressed in the stomach; however no expression is detected in cancer tissue or gastric cancer cell lines.
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Synonyms
BRICHOS domain containing 1, 18 kDa antrum mucosa protein, gastrokine 1, Protein CA11, AMP-18, BRICD1, foveolin, FOV.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSH MLAYSS VHCFREDKMK FTIVFAGLLG VFLAPALANY NINVNDDNNN AGSGQQSVSV NNEHNVANVD NNNGWDSWNS IWDYGNGFAA TRLFQKKTCI VHKMNKEVMP SIQSLDALVK EKKLQGKGPG GPPPKGLMYS VNPNKVDDLS KFGKNIANMC RGIPTYMAEE MQEASLFFYS GTCYTTSVLW IVDISFCGDT VEN.
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 :
VAMP2 Human, (1-94)Description:
Synaptobrevin-2 Human Recombinant, (1-94)
Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.
Product # :
PRO-2644Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VAMP2 Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-94 a.a) and having a molecular mass of 12.8kDa. VAMP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.Coli
Formulation
The VAMP2 solution (0.5mg/1ml) contains 0.1mM PMSF, 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Synaptobrevin-2 or VAMP2 is a protein that has a proline-rich N-terminal part, highly conserved hydrophilic domain, a transmembrane anchor and a C-terminal.VAMP2 found in the transmembrane region of the cell, in the cytoplasmic surface of the synaptic vesicle. The protein is mainly found in the Langerhans islets in the pancreas and glomerular cells in the kidney. A SNARE complex is created within the protein’s N-terminal domain and the target membrane-associated T.
-
Synonyms
Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSATAA TAPPAAPAGE GGPPAPPPNL TSNRRLQQTQ AQVDEVVDIM RVNVDKVLER DQKLSELDDR ADALQAGASQ FETSAAKLKR KYWWKNLK.
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 :
RAB22A HumanDescription:
RAB22, Member RAS Oncogene Family Recombinant Human
Ras-related protein Rab-22A, Rab-22, RAB22A, RAB22, MGC16770.
Product # :
PRO-929Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RAB22A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 214 amino acids (1-194 a.a.) and having a molecular mass of 24kDa.RAB22A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RAB22A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ras-related protein Rab-22A (RAB22A) belongs to the RAB family of small GTPases. The GTP-bound form of the RAB22A interacts with early-endosomal antigen 1, and may be involved in the transferring of and interaction between endosomal compartments.
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Synonyms
Ras-related protein Rab-22A, Rab-22, RAB22A, RAB22, MGC16770.
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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 MALRELKVCL LGDTGVGKSS IVWRFVEDSF DPNINPTIGA SFMTKTVQYQ NELHKFLIWD TAGQERFRAL APMYYRGSAA AIIVYDITKE ETFSTLKNWV KELRQHGPPN IVVAIAGNKC DLIDVREVME RDAKDYADSI HAIFVETSAK NAININELFI EISRRIPSTD ANLPSGGKGF KLRRQPSEPK RSCC.
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 :
LFA 3 HumanDescription:
Lymphocyte Function Associated Antigen-3 Human Recombinant , Fusion Protein
CD58, LFA-3, Ag3, Surface glycoprotein LFA-3.
Product # :
CYT-423Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Lymphocyte Function-Associated Antigen-3 Fusion Protein Recombinant Human is produced by recombinant DNA technology in a Chinese Hamster Ovary (CHO) mammalian cell expression system. The molecular weight is 91.4 kDa. Recombinant LFA3 is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary.
Formulation
Each mg of CD58 contains 0.8mg sucrose, 0.3mg glycine, 0.25mg sodium citrate dihydrate, and 4µg citric acid monohydrate.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
LFA-3 is ligand of the t-lymphocyte cd2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and dependent interactions of t-lymphocytes with target cells and antigen- presenting cells and the t-lymphocyte rosetting with erythrocytes. In addition, the lfa-3/cd2 interaction may prime response by both the cd2+ and lfa-3+ cells.
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Synonyms
CD58, LFA-3, Ag3, Surface glycoprotein LFA-3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LFA3 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human LFA-3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized LFA-3 Human 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 :
Cys-Protein-GDescription:
Cys-Protein G Recombinant
Product # :
PRO-1238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cys-Protein G Recombinant produced in E.Coli, is a single non-glycosylated polypeptide chain containing 201 amino acids and having a cys on N-terminal. Cys-Protein G has a predicted molecular mass of approximately 21.9kDa but it migrates with an apparent molecular mass of 40kDa in SDS-PAGE. The Cys-Protein G is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized without any additives.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Citations
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G 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 Protein G in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CLPKTDTYKL ILNGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTKAVDAET AEKAFKQYAN DNGVDGVWTY DDATKTFTVT E.
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Specificity
The recombinant Protein G is a genetically engineered protein contains 3 IgG-binding regions of protein G.
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 :
CRYAA HumanDescription:
Crystallin Alpha A Human Recombinant
CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein beta-4.
Product # :
HSP-002Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human CRYAA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids and having a molecular mass of 19.9kDa.CRYAA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYAA protein contains 20mM Tris-HCl buffer (pH 7.5), 50mM NaCl and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein(sHSP also known as the HSP20). They act as molecular chaperones and hold them in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. The expression of alpha-A is preferentially restricted to the lens cell.
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Synonyms
CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein 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
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSGISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRLPSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS.
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 :
Trypsin BovineDescription:
Trypsin Bovine Recombinant
Product # :
PRO-313Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- biological activity
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Description
Recombinant Bovine Trypsin is free from any animal and human sources. Trypsin Bovine specifically cleaves peptide bonds after basic amino acids such as lysine and arginine.
Source
Corn.
Formulation
The protein was lyophilized without any additives.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
4,313 Units/mg.
Citations
More Info
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Introduction
Trypsin is a serine protease that hydrolyses proteins, it is found in the digestive system of numerous vertebrates. Trypsin is produced as the inactive proenzyme trypsinogen in the pancreas. Trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline. Trypsin is secreted into the duodenum, where it acts to hydrolyses peptides into amino acids, which is necessary for the uptake of protein in the food even though peptides are smaller than proteins; they are still too big to be absorbed through the lining of the ileum. The optimal operating pH for Trypsins is about 8 and about 37°C temperature. In cystic fibrosis disease there is a deficiency in transport of trypsin and other digestive enzymes from the pancreas. Trypsin is widely used in various biotechnological processes since it’s available in high quantity in the pancreases, and can be purified rather easily.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Store the Bovine Trypsin between 2-8°C, do not freeze.
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Solubility
It is recommended to reconstitute the lyophilized Bovine Trypsin 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 :
ADRM1 HumanDescription:
Adhesion Regulating Molecule 1 Human Recombinant
Proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, Gp110, Adhesion-regulating molecule 1, ARM-1, Proteasome regulatory particle non-ATPase 13, hRpn13, Rpn13 homolog, ADRM1, ARM1, Rpn13.
Product # :
PRO-1079Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ADRM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 431 amino acids (1-407 a.a) and having a molecular mass of 44.7kDa.ADRM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ADRM1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Proteasomal ubiquitin receptor ADRM1 (ADRM1) functions as a proteasomal ubiquitin receptor. ADRM1 is an integral plasma membrane protein which promotes cell adhesion. ADRM1 is assumed to undergo O-linked glycosylation. ADRM1 employs the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.
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Synonyms
Proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, Gp110, Adhesion-regulating molecule 1, ARM-1, Proteasome regulatory particle non-ATPase 13, hRpn13, Rpn13 homolog, ADRM1, ARM1, Rpn13.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTTSGA LFPSLVPGSR GASNKYLVEF RAGKMSLKGT TVTPDKRKGL VYIQQTDDSL IHFCWKDRTS GNVEDDLIIF PDDCEFKRVP QCPSGRVYVL KFKAGSKRLF FWMQEPKTDQ DEEHCRKVNE YLNNPPMPGA LGASGSSGHE LSALGGEGGL QSLLGNMSHS QLMQLIGPAG LGGLGGLGAL TGPGLASLLG SSGPPGSSSS SSSRSQSAAV TPSSTTSSTR ATPAPSAPAA ASATSPSPAP SSGNGASTAA SPTQPIQLSD LQSILATMNV PAGPAGGQQV DLASVLTPEI MAPILANADV QERLLPYLPS GESLPQTADE IQNTLTSPQF QQALGMFSAA LASGQLGPLM CQFGLPAEAV EAANKGDVEA FAKAMQNNAK PEQKEGDTKD KKDEEEDMSL D.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.