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Description:

Epidermal Growth Factor Mouse Recombinant, His Tag

Urogastrone, URG, EGF.

Product # :

CYT-138

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SDS-PAGE

Description

EGF mouse Recombinant produced in E. coli is a single polypeptide chain containing 77 amino acids (977-1029) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EGF solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
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 MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
Background
Unveiling Epidermal Growth Factor Mouse Recombinant: Harnessing His Tag for Enhanced Insights and Therapeutic Prospects
Abstract:
This research paper delves into the realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), focusing on the strategic integration of a Histidine (His) Tag. By employing sophisticated methodologies encompassing protein engineering, chromatographic techniques, and cellular assays, this study unveils the multifaceted molecular attributes of EGF-MR with His Tag. The findings not only enhance our understanding of EGF-MR's behavior but also illuminate potential avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) governs vital cellular processes. This paper delves into Epidermal Growth Factor Mouse Recombinant (EGF-MR) with a specific emphasis on the incorporation of a Histidine (His) Tag, unraveling its molecular intricacies and therapeutic implications.
Protein Engineering and His Tag Integration:
The paper navigates the tailored engineering of EGF-MR to accommodate a His Tag, a peptide sequence that facilitates protein purification. The process involves strategic modification of the EGF-MR gene to ensure proper folding and presentation of the His Tag.
Chromatographic Purification and His Tag Affinity:
Chromatographic techniques, specifically immobilized metal ion affinity chromatography (IMAC), are employed to purify the His-tagged EGF-MR. The His Tag's high affinity for metal ions facilitates efficient purification, yielding a highly purified and bioactive protein product.
Structural and Functional Insights:
The presence of the His Tag is not just for purification; it serves as a molecular handle to investigate EGF-MR's structural dynamics. High-resolution structural analyses coupled with biophysical assays unravel how the His Tag affects EGF-MR's conformation and binding interactions.
Cellular Assays and Bioactivity Assessment:
In vitro cellular assays, including proliferation and migration studies, provide insights into the impact of His Tag on EGF-MR's bioactivity. Comparative analyses shed light on the functionality of His-tagged EGF-MR and its potential implications in cellular responses.
Therapeutic Prospects and Targeted Delivery:
The incorporation of a His Tag presents a unique avenue for tailored drug delivery. The His Tag can serve as a docking site for targeted therapies, enabling precise interactions with specific receptors on target cells.
Future Directions and Challenges:
While promising, challenges such as potential steric hindrance from the His Tag require consideration. Future research should focus on optimizing the positioning of the His Tag to maintain EGF-MR's full biological activity.
Conclusion:
In a harmonious synthesis of advanced methodologies and innovative insights, the integration of His Tag into Epidermal Growth Factor Mouse Recombinant emerges as a transformative paradigm. The His Tag not only facilitates purification but also offers a molecular window into EGF-MR's behavior, potentially redefining targeted therapies and precision medicine.
What is the molecular weight/Mw of EGF MOUSE, HIS Protein?
EGF MOUSE, HIS Protein has a total Mw of 8.6kDa.

What is the source or expression system of EGF MOUSE, HIS Protein?
Escherichia Coli.

What is the Purity of EGF MOUSE, HIS Protein?
EGF MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF MOUSE, HIS Protein?
The biological functionality of EGF MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of EGF MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

What applications can EGF MOUSE, HIS Protein be used in?
EGF MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF MOUSE, HIS Protein?
The endotoxin level is minimal, EGF MOUSE, HIS 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.

Description:

NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 1 Human Recombinant

Complex I intermediate-associated protein 30, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1, NDUFAF1, CIA30, CGI-65, CGI65.

Product # :

ENZ-661

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Description

NDUFAF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 326 amino acids (25-327) and having a molecular mass of 37kDa.NDUFAF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NDUFAF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4 (NDUFAF4) is involved in the compilation of mitochondrial NADH: ubiquinone oxidoreductase complex (complex I). In addition, NDUFAF4 is involved in cell proliferation and survival of hormone-dependent tumor cells. NDUFAF4 may also be a regulator of breast tumor cell invasion. NDUFAF4 gene mutations cause the mitochondrial complex I deficiency.
Synonyms
Complex I intermediate-associated protein 30, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1, NDUFAF1, CIA30, CGI-65, CGI65.
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 MGSYPFLGIR FAEYSSSLQK PVASPGKASS QRKTEGDLQG DHQKEVALDI TSSEEKPDVS FDKAIRDEAI YHFRLLKDEI VDHWRGPEGH PLHEVLLEQA KVVWQFRGKE DLDKWTVTSD KTIGGRSEVF LKMGKNNQSA LLYGTLSSEA PQDGESTRSG YCAMISRIPR GAFERKMSYD WSQFNTLYLR VRGDGRPWMV NIKEDTDFFQ RTNQMYSYFM FTRGGPYWQE VKIPFSKFFF SNRGRIRDVQ HELPLDKISS IGFTLADKVD GPFFLEIDFI GVFTDPAHTE EFAYENSPEL NPRLFK.

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.

Description:

Cardiac Troponin-I Chimeric Human Recombinant

Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

Product # :

PRO-2790

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Description

TNNI3 Human Chimeric produced in E.Coli is a single, non-glycosylated polypeptide chain (28-110 a.a.) and having a molecular mass of 29072 Dalton.

Source

Escherichia Coli.

Formulation

TNNI3 was lyophilized in 50mM Tris-HCl, 5mM Calcium chloride, 0.7M KCl and 0.1% 2-mercaptoethanol, pH 7.5

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cardiac Troponin-I Chimeric although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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 TNNI3 in buffer containing BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Troponin I (TNNI3) is a crucial regulatory protein in cardiac muscle, playing a central role in the regulation of muscle contraction. Understanding the structure and function of TNNI3 is essential for unraveling the complexities of cardiac muscle physiology and exploring therapeutic interventions for cardiac diseases. Chimeric TNNI3 proteins, which combine segments from different isoforms or species, offer a unique opportunity to investigate the role of specific regions in TNNI3 function and to potentially develop novel therapies. This research aims to provide a comprehensive exploration of chimeric TNNI3 proteins, elucidating their functions, structural significance, and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the functional significance of chimeric TNNI3 proteins in cardiac muscle. In vitro and ex vivo experiments, utilizing engineered chimeric TNNI3 constructs and cardiac tissue models, will be conducted to investigate how these proteins influence muscle contractility, calcium sensitivity, and response to pathological conditions. Understanding these mechanisms is fundamental for deciphering the roles of specific TNNI3 regions in cardiac muscle function.
The second objective is to assess the therapeutic potential of chimeric TNNI3 proteins in cardiac diseases. Experimental studies involving animal models and cellular systems will explore the use of chimeric TNNI3 proteins as potential therapeutic agents for heart conditions. These investigations may provide valuable insights into novel treatment strategies targeting cardiac muscle function.
The third objective is to explore the broader applications of chimeric TNNI3 proteins in biotechnology and drug development. Research will investigate the use of chimeric TNNI3-expressing cells and tissues as models for studying cardiac disorders and for developing innovative approaches in regenerative medicine and pharmacology.
By delving into the functions and roles of chimeric TNNI3 proteins, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology, biotechnology, and drug development

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.

Description:

Insulin Like Growth Factor Binding Protein-7Human Recombinant, His Tag

Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.

Product # :

CYT-809

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Description

IGFBP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (27-282 a.a.) and having a molecular mass of 28.8kDa.IGFBP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGFBP7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 1mM EDTA.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Insulin-like Growth Factor-Binding Protein 7 (IGFBP7) is a member of the IGFBP family. IGFBP family members are all cysteine rich proteins with conserved cysteine and have an IGFBP domain, a Kazal-like domain and an Ig-like C2-type domain. IGFBP7 is expressed in a broad range of normal human tissues and it mostly shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. IGFBP7 has a role in skeletal myogenesis by binding to IGF in a manner which inhibits IGF induced differentiation of skeletal myoblasts, without disturbing IGF induced proliferation. Moreover, IGFBP7 suppresses growth and colony formation of prostate and breast cancer cell lines via an IGF independent mechanism, which triggers a delay in the G1 phase of the cell cycle, and increased apoptosis.
Synonyms
Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.
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 MGSSSSDTCG PCEPASCPPL PPLGCLLGET RDACGCCPMC ARGEGEPCGG GGAGRGYCAP GMECVKSRKR RKGKAGAAAG GPGVSGVCVC KSRYPVCGSD GTTYPSGCQL RAASQRAESR GEKAITQVSK GTCEQGPSIV TPPKDIWNVT GAQVYLSCEV IGIPTPVLIW NKVKRGHYGV QRTELLPGDR DNLAIQTRGG PEKHEVTGWV LVSPLSKEDA GEYECHASNS QGQASASAKI TVVDALHEIP VKKGEGAEL.

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Description:

ASF1 Anti-Silencing Function 1 Homolog B Human Recombinant

Histone chaperone ASF1B, Anti-silencing function protein 1 homolog B, hAsf1, hAsf1b, CCG1-interacting factor A-II, CIA-II, hCIA-II, ASF1B.

Product # :

PRO-1163

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Description

ASF1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-202 a.a) and having a molecular mass of 23.4kDa.ASF1B is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ASF1B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
ASF1 Anti-Silencing Function 1 Homolog B (ASF1B) belongs to the H3/H4 family of histone chaperone proteins and is similar to the anti-silencing function-1 protein in yeast. ASF1B is the substrate of the tousled-like kinase family of cell cycle-regulated kinases, and may have a crucial role in modulating the nucleosome structure of chromatin by guaranteeing a regular supply of histones at sites of nucleosome assembly. ASF1B cooperates with CAF-1 (chromatin assembly factor 1) to stimulate replication-dependent chromatin assembly. ASF1B is highly expressed in the testis and at lower levels in colon, small intestine and thymus. ASF1B is necessary for spermatogenesis.
Synonyms
Histone chaperone ASF1B, Anti-silencing function protein 1 homolog B, hAsf1, hAsf1b, CCG1-interacting factor A-II, CIA-II, hCIA-II, ASF1B.
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
MAKVSVLNVA VLENPSPFHS PFRFEISFEC SEALADDLEW KIIYVGSAES EEFDQILDSV LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT YHGQEFIRVG YYVNNEYLNP ELRENPPMKP DFSQLQRNIL ASNPRVTRFH INWDNNMDRL EAIETQDPSL GCGLPLNCTP
IKGLGLPGCI PGLLPENSMD CILEHHHHHH.

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.

Description:

Deoxyribose-Phosphate Aldolase Human Recombinant

Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.

Product # :

ENZ-170

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Description

DERA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (1-318) and having a molecular mass of 37.3 kDa.DERA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The DERA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Deoxyribose-phosphate aldolase (DERA) is a member of the deoC/fbaB aldolase protein family involved in the carbohydrate degradation pathway. DERA catalyzes the conversion of 2-deoxy-D-ribose 5-phosphate to D-glyceraldehyde 3-phosphate and an acetyldehyde.
Synonyms
Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.
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 MSAHNRGTEL DLSWISKIQV NHPAVLRRAE QIQARRTVKK EWQAAWLLKA VTFIDLTTLS GDDTSSNIQR LCYKAKYPIR EDLLKALNMH DKGITTAAVC VYPARVCDAV KALKAAGCNI PVASVAAGFP AGQTHLKTRL EEIRLAVEDG ATEIDVVINR SLVLTGQWEA LYDEIRQFRK ACGEAHLKTI LATGELGTLT NVYKASMIAM MAGSDFIKTS TGKETVNATF PVAIVMLRAI RDFFWKTGNK IGFKPAGGIR SAKDSLAWLS LVKEELGDEW LKPELFRIGA STLLSDIERQ IYHHVTGRYA AYHDLPMS

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.

Description:

Lysophospholipase II Human Recombinant

Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.

Product # :

ENZ-076

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Description

LYPLA2 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 251 amino acids (1-231 a.a.) and having a molecular mass of 26.9kDa. The LYPLA2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LYPLA2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Acyl-protein thioesterase 2 (LYPLA2) is lysophospholipase which acts on biological membranes to regulate the multifunctional lysophospholipids. LYPLA2 may hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS.
Synonyms
Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.
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 MCGNTMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRAFPQAAN GSAKDLAILQ CHGELDPMVP VRFGALTAEK LRSVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V.

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.

Description:

Glutathione S-Transferase Alpha 4 Human Recombinant, Active

Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.

Product # :

ENZ-996

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Description

GSTA4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-222) and having a molecular mass of 28.3kDa.GSTA4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GSTA4 solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 20% glycerol, 2mM DTT and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 4,000 pmol/min/ug, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4- dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

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Introduction
Glutathione S-transferase A4 (GSTA4) is a member of the GST superfamily. The GSTA4 enzyme is involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. GSTA4 shows an especially high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is extremely effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, which is an important product of peroxidative degradation of arachidonic acid and a frequently used biomarker for oxidative damage in tissue. The GSTA4 enzyme is expressed at a high level in the brain, placenta, and skeletal muscle and much lower in the lung and liver.
Synonyms
Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.
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 MGSHMAARPK LHYPNGRGRM ESVRWVLAAA GVEFDEEFLE TKEQLYKLQD GNHLLFQQVP MVEIDGMKLV QTRSILHYIA DKHNLFGKNL KERTLIDMYV EGTLDLLELL IMHPFLKPDD QQKEVVNMAQ KAIIRYFPVF EKILRGHGQS FLVGNQLSLA DVILLQTILA LEEKIPNILS AFPFLQEYTV KLSNIPTIKR FLEPGSKKKP PPDEIYVRTV YNIFRP.

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.

Description:

Glutamic-Oxaloacetic Transaminase 2, Active Mouse Recombinant

Transaminase A, KAT4, KATIV, KAT-4, KAT-IV, Kynurenine Aminotransferase 4.

Product # :

ENZ-1111

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Description

GOT2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (30-430 aa) and having a molecular mass of 46.8kDa.GOT2 is fused to a 21 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GOT2 solution (0.5 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH7.4)

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 20 units/mg. Measured by the amount of enzyme that converts 1umole of alpha-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C˚.

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Introduction
GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 participates in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.
Synonyms
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV, Kynurenine Aminotransferase 4.
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 MSSWWTHVEM GPPDPILGVT EAFKRDTNSK KMNLGVGAYR
DDNGKPYVLP SVRKAEAQIA AKNLDKEYLP IGGLAEFCKA SAELALGENN EVLKSGRFVT
VQTISGTGAL RVGASFLQRF FKFSRDVFLP KPSWGNHTPI FRDAGMQLQG YRYYDPKTCG
FDFSGALEDI SKIPEQSVLL LHACAHNPTG VDPRPEQWKE IASVVKKKNL FAFFDMAYQG
FASGDGDKDA WAVRHFIEQG INVCLCQSYA KNMGLYGERV GAFTVVCKDA EEAKRVESQL
KILIRPLYSN PPLNGARIAA TILTSPDLRK QWLQEVKGMA DRIISMRTQL VSNLKKEGSS
HNWQHITDQI GMFCFTGLKP EQVERLTKEF SVYMTKDGRI SVAGVTSGNV GYLAHAIHQV TK

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.

Description:

High Density Lipoprotein Human

High Density Lipoprotein, HDL.

Product # :

PRO-559

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Description

Human High Density Lipoprotein (HDL) produced in Human plasma.

Source

Human plasma.

Purity

Cholesterol level >200mg/l. <1% LDL.

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Introduction
HDL is a complex of lipids and proteins in approximately equal amounts that functions as a transporter of cholesterol in the blood. HDL is the smallest of the lipoprotein particles; it’s the densest because it contains the highest proportion of protein. The liver synthesizes these lipoproteins as complexes of apolipoproteins and phospholipid, which bear a resemblance to cholesterol-free flattened spherical lipoprotein particles. They pick up cholesterol; carry it internally, from cells by interaction with the ATP Binding Cassette Transporter A1. Lecithin-cholesterol acyltransferase (plasma enzyme) converts the free cholesterol into cholesteryl ester (a more hydrophobic form of cholesterol) which is then sequestered into the core of the lipoprotein particle ultimately making the newly synthesized HDL spherical. They increase in size as they pass through the bloodstream and integrate more cholesterol and phospholipid molecules from cells and other lipoproteins, for instance by the interaction with the ABCG1 transporter and the phospholipid transport protein. HDL transports their cholesterol generally to the liver or steroidogenic organs such as adrenals, ovary and testes by direct and indirect pathways. The release of HDL cholesterol to adrenals, ovaries and testes is important for the synthesis of steroid hormones. Since the triglycerides are not stable in HDL, they’re degraded by hepatic lipase in order that finally small HDL particles are left which resume the uptake of cholesterol from cells. The cholesterol supplied to the liver is excreted into the bile and consequently intestine either directly or indirectly after conversion into bile acids. High levels of HDL are associated with a decreased risk of atherosclerosis and coronary heart disease.
Synonyms
High Density Lipoprotein, HDL.
Physical Appearance
Yellow to orange liquid.
Stability
Human HDL although stable at 4°C for 1 week, should be stored below -15°C (short term i.e. < 3 months) and below -70°C for long term.
Human Virus Test
Starting material donor tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, Hepatitis C antibodies, HIV1/HCV/HBV NAT and Syphilis.

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.

Description:

Allergenic Isoflavone Reductase-Like Protein Bet v 6.0102 Recombinant

Allergenic isoflavone reductase-like protein Bet v 6.0102, BETV6.0102.

Product # :

ALR-018

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Description

Recombinant BETV6.0102 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 36,636 Dalton. BETV6.0102 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

BETV6.0102 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
BETV6.0102 allergen is one of Isoflavone reductases which were found in pear, orange, apple, mango, lychee and other plants. Isoflavone reductases are plant defense proteins which induced by plant stress, e.g. high salinity, freeze or drought.
Synonyms
Allergenic isoflavone reductase-like protein Bet v 6.0102, BETV6.0102.
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. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

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.

Description:

Annexin A10 (1-162 a.a.) Human Recombinant

anxa-10.

Product # :

PRO-2837

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Description

The ANXA10 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The ANXA10 His-Tagged Fusion Protein, produced in E. coli, is a 21kDa protein containing 162 amino acid residues of the ANXA10 Human, 1-162 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
anxa-10.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized ANXA10 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Annexin A10 also known as ANXA10 is a part of the annexin family of calcium-binding proteins which members own a conserved core domain and a unique amino-terminal region which may convene binding specificity. The ANXA10 protein contains 4 annexin domains and plays a role in the regulation of cellular growth and signal transduction pathways throughout the cell.

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.

Description:

Xylosyltransferase 2 Human Recombinant

Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.

Product # :

ENZ-1086

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Description

XYLT2 Human Recombinant is a single, glycosylated polypeptide chain containing 839 amino acids (Gly37-Arg865, luminal domain, isoform 1, natural variant with Thr305) and having a molecular mass of 94.0kDa. XYLT2 is fused to an N-terminal linker (2 extra a.a), C-terminal linker (2 extra a.a) and C-terminal His-tag (6 extra a.a).

Source

HEK293 Cells.

Formulation

XYLT2 filtered (0.4 µm) and lyophilized in 0.05 M PBS and 0.075 M NaCl, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
XYLT2 or Xylosyltransferase 2 is an enzyme which is expressed in ubiquitous and is part of the glycosyltransfe-rases family. XYLT2 promotes proteoglycans formation by attaching GAG chains to the substrate protein via transfer of xylose molecule from the donor (nucleoside diphosphate) to the protein’s serine residues. XYLT2 is present in the ER and the cis part of the Golgi, furthermore the protein is released to the extracellular matrix.
Synonyms
Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.
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 0.5mg/ml and let the lyophilized pellet dissolve completely. XYLT2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
ASGLEEDEAG EKGRQRKPRP LDPGEGSKDT DSSAGRRGST GRRHGRWRGR AESPGVPVAK VVRAVTSRQR ASRRVPPAPP PEAPGRQNLS GAAAGEALVG AAGFPPHGDT GSVEGAPQPT DNGFTPKCEI VGKDALSALA RASTKQCQQE IANVVCLHQA GSLMPKAVPR HCQLTGKMSP GIQWDESQAQ QPMDGPPVRI AYMLVVHGRA IRQLKRLLKA VYHEQHFFYI HVDKRSDYLH REVVELAQGY DNVRVTPWRM VTIWGGASLL TMYLRSMRDL LEVPGWAWDF FINLSATDYP TRTNEELVAF LSKNRDKNFL KSHGRDNSRF IKKQGLDRLF HECDSHMWRL GERQIPAGIV VDGGSDWFVL TRSFVEYVVY TDDPLVAQLR QFYTYTLLPA ESFFHTVLEN SLACETLVDN NLRVTNWNRK LGCKCQYKHI VDWCGCSPND FKPQDFLRLQ QVSRPTFFAR KFESTVNQEV LEILDFHLYG SYPPGTPALK AYWENTYDAA DGPSGLSDVM LTAYTAFARL SLHHAATAAP PMGTPLCRFE PRGLPSSVHL YFYDDHFQGY LVTQAVQPSA QGPAETLEMW LMPQGSLKLL GRSDQASRLQ SLEVGTDWDP KERLFRNFGG LLGPLDEPVA VQRWARGPNL TATVVWIDPT YVVATSYDIT VDTETEVTQY KPPLSRPLRP GPWTVRLLQF WEPLGETRFL VLPLTFNRKL PLRKDDASWL HAGPPHNEYM EQSFQGLSSI LNLPQPELAE EAAQRHTQLT GPALEAWTDR ELSSFWSVAG LCAIGPSPCP SLEPCRLTSW SSLSPDPKSE LGPVKADGRL RKLHHHHHH.

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.

Description:

Complement C5 Human

Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.

Product # :

PRO-2691

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Description

Human Complement C5 produced in Human plasma having a molecular mass of 190 kDa.

Source

Human Plasma.

Formulation

C5 protein solution contains PBS, pH 7.2.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Complement C5 is cleaved into C5a and C5b and is activated by all 3 pathways of complement activation. Each pathway of complement activation generates proteolytic enzyme complexes which binds to the target surface. These enzymes cleave a peptide bond in the larger alpha chain of C5 releasing the highly potent anaphylatoxin C5a and activating C5b. C5a has an imperative role in chemotaxis and C5b forms the 1st part of the complement membrane attack complex. Complement C5 is the 5th component of complement, which plays a central role in inflammatory and cell killing processes.
Synonyms
Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.
Physical Appearance
Sterile filtered solution.
Stability
C5 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HTLV-I &II, Syphillis and HBSAG.

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.

Description:

Inhibitor of Growth Family, Member 2 Human Recombinant

Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

Product # :

PRO-1739

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Description

ING2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 35.2kDa.ING2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ING2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).
Synonyms
Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.
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 MGSMLGQQQQ QLYSSAALLT GERSRLLTCY VQDYLECVES LPHDMQRNVS VLRELDNKYQ ETLKEIDDVY EKYKKEDDLN QKKRLQQLLQ RALINSQELG DEKIQIVTQM LELVENRARQ MELHSQCFQD PAESERASDK AKMDSSQPER SSRRPRRQRT SESRDLCHMA NGIEDCDDQP PKEKKSKSAK KKKRSKAKQE REASPVEFAI DPNEPTYCLC NQVSYGEMIG CDNEQCPIEW FHFSCVSLTY KPKGKWYCPK CRGDNEKTMD KSTEKTKKDR RSR.

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.

Description:

Platelet Factor-4 Variant 1 Human Recombinant

CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

Product # :

CHM-243

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Description

CXCL4 Variant-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized without additives.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets . Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily. Human PF4 is used for the proof of induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.

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.

Description:

Epidermal Growth Factor Mouse Recombinant, Biotin

Urogastrone, URG, EGF.

Product # :

CYT-841

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Description

EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.

Source

Escherichia Coli.

Formulation

The protein (0.5mg/ml) solution contains sterile PBS.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x10⁶units/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered clear solution.
Stability
Should be stored at 4°C.Please do not freeze.
Amino Acid Sequence
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.
Background
Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential
Abstract:
This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.
Introduction:
Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.
Protein Engineering and Biotin Conjugation:
EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.
Cellular Signaling Amplification:
The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.
Cellular Assays and Functional Responses:
In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.
Tailored Delivery Strategies:
The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.
Regenerative Medicine and Targeted Therapy:
The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.
Future Prospects and Challenges:
While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.
Conclusion:
In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.
What is the molecular weight/Mw of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein has a total Mw of 7kDa.

What is the source or expression system of MEGF, BIOTIN Protein?
Escherichia Coli.

What is the Purity of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of MEGF, BIOTIN Protein?
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

What is the amino acid sequence of MEGF, BIOTIN Protein?
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

What applications can MEGF, BIOTIN Protein be used in?
MEGF, BIOTIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for MEGF, BIOTIN Protein?
The endotoxin level is minimal, MEGF, BIOTIN 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.

Description:

Pigment Epithelium-Derived Factor Human Recombinant, HEK

Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

Product # :

CYT-553

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Description

PEDF Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 410 amino acids, having a molecular mass of 45.6 kDa and fused to an 11 aa FLAG tag at C-Terminus.The Human PEDF is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

The filtered (0.4µm) concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
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.
Solubility
It is recomnded to add deionized water to a working concentration of 0.5mg/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
QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGPAAADYKDDDDK.

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.

Description:

GM-CSF Receptor Alpha Sf9 Human Recombinant

Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.

Product # :

CYT-1044

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Description

CSF2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (20-320a.a.) and having a molecular mass of 35.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CSF2RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CSF2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

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Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
Synonyms
Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.
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
ADPLIPEKSD LRTVAPASSL NVRFDSRTMN LSWDCQENTT FSKCFLTDKK NRVVEPRLSN NECSCTFREI CLHEGVTFEV HVNTSQRGFQ QKLLYPNSGR EGTAAQNFSC FIYNADLMNC TWARGPTAPR DVQYFLYIRN SKRRREIRCP YYIQDSGTHV GCHLDNLSGL TSRNYFLVNG TSREIGIQFF DSLLDTKKIE RFNPPSNVTV RCNTTHCLVR WKQPRTYQKL SYLDFQYQLD VHRKNTQPGT ENLLINVSGD LENRYNFPSS EPRAKHSVKI RAADVRILNW SSWSEAIEFG SDDGHHHHHH
Background
GM-CSF Receptor Alpha Human Recombinant: A Glimpse into Its Potential and Implications
Abstract:
Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) receptor alpha, a pivotal component in the GM-CSF signaling pathway, has been the focal point of numerous studies pertaining to hematopoiesis and immune responses. This paper provides an overview of the GM-CSF receptor alpha human recombinant, exploring its characteristics, production techniques, and potential therapeutic applications.
Introduction
GM-CSF, a cytokine responsible for the differentiation and proliferation of white blood cells, functions by binding to its receptor, GM-CSF receptor. The alpha subunit (GM-CSFRα) of this receptor plays a crucial role in ligand binding and is essential for initiating cellular responses. Modern biotechnological advancements have led to the successful production of its human recombinant form, offering new avenues in medical research.
Recombinant GM-CSFRα:
Production and Features Recombinant GM-CSFRα is synthesized using cutting-edge recombinant DNA technologies, predominantly in bacterial or mammalian expression systems. This human recombinant form retains its ability to bind to GM-CSF, maintaining its biological functionality and providing myriad research opportunities.
Therapeutic and Clinical Prospects
1. Autoimmune Diseases: GM-CSF is often overexpressed in various autoimmune disorders. By utilizing recombinant GM-CSFRα as a potential decoy receptor, it's feasible to mitigate the effects of excessive GM-CSF, offering a new therapeutic strategy.
2. Hematopoietic Disorders: Given its integral role in white blood cell development, recombinant GM-CSFRα might hold promise in treatments or as a diagnostic tool for certain hematological conditions.
3. Research Paradigm: Beyond therapeutic applications, the recombinant GM-CSFRα can serve as an invaluable research tool to elucidate the nuances of GM-CSF signaling, aiding in the understanding of immune response mechanisms.
Conclusion:
GM-CSF receptor alpha human recombinant stands at the forefront of exciting research and therapeutic potential. While its full capabilities are yet to be realized, current insights underscore its significance in the realms of immunology and medicine.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 35.9kDa.

What is the source or expression system of CD116 Protein?
Sf9, Baculovirus cells.
What is the Purity of CD116 Protein?
CD116 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CD116 Protein?
Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 310 amino acids.

What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 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.

Description:

Transforming Growth Factor-Beta 3 Rat Recombinant

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-1269

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Description

TGFB3 Rat Recombinant produced in CHO cells is a glycosylated, polypeptide homodimer chain containing 2x112 amino acids and having a total molecular mass of 25.0kDa. The TGFB3 is purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

TGFB3 was lyophilized from a concentrated solution containing 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

Purity

Greater than 97.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by its ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Transforming Growth Factor-Beta 3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 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 TGFB3 in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSSDTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Background
Recombinant TGF-β3 Rat is commonly used in cell culture and biomedical research to investigate TGF-β signalling, stem cell differentiation, tissue engineering, chondrogenesis, wound healing, fibrosis, and cancer biology. TGFB3 is added to mesenchymal stem cell and chondrocyte cultures to promote cartilage formation and maintain specific cellular phenotypes under defined experimental conditions.

What is the molecular weight / Mw of TGFB3 Rat Protein?
TGFB3 Rat Protein has a total Mw of 25kDa.

What is the source or expression system of TGFB3 Rat Protein?
CHO Cells

What is the Purity of TGFB3 Rat Protein?
TGFB3 rat Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of TGFB3 rat Protein?
Determined by the ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0×107 units/mg.

What is the amino acid sequence of TGFB3 Protein?
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS

What applications can TGFB3 rat Protein be used in?
TGFB3 rat Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for TGFB3 rat Protein?
The endotoxin level is minimal, TGFB3 rat Protein was purified using conventional chromatography techniques.

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Description:

Bovine Collagen-I

Product # :

PRO-2680

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Description

Bovine Collagen-I is a natural protein purified from bovine skin. Collagen-I is purified by proprietary chromatographic techniques.

Source

Bovine skin.

Formulation

Collagen-I was lyophilized without additives.

Purity

> 90.0%.

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Introduction
Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Collagen-I although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-I should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to Add 0.5M acetic acid to prepare a working stock solution of approximately 1-5mg/ml and let the lyophilized pellet dissolve completely.

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Description:

TRAF Family Member-Associated NFKB Activator Human Recombinant

TRAF, TRAF2, TRAF-interacting protein, ITRAF.

Product # :

PRO-1348

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Shipped with Ice Packs

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Description

TANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 448 amino acids (1-425a.a) and having a molecular mass of 50.2kDa. TANK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TANK protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
TRAF Family Member-Associated NFKB Activator (TANK) is located in the cytoplasm and binds Either TRAF1, TRAF2 or TRAF3. TANK is an inhibitor of TRAF function which regulates TRAF protein activity via sequestering TRAFs in a dormant position in the cytoplasm. Overexpression of TANK, inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and also inhibits LMP1-mediated NFkappa-B activation by blocking the connection of TRAF2 with LMP1.
Synonyms
TRAF, TRAF2, TRAF-interacting protein, ITRAF.
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 MGSMDKNIGE QLNKAYEAFR QACMDRDSAV KELQQKTENY EQRIREQQEQ LSLQQTIIDK LKSQLLLVNS TQDNNYGCVP LLEDSETRKN NLTLDQPQDK VISGIAREKL PKVRRQEVSS PRKETSARSL GSPLLHERGN IEKTFWDLKE EFHKICMLAK AQKDHLSKLN IPDTATETQC SVPIQCTDKT DKQEALFKPQ AKDDINRGAP SITSVTPRGL CRDEEDTSFE SLSKFNVKFP PMDNDSTFLH STPERPGILS PATSEAVCQE KFNMEFRDNP GNFVKTEETL FEIQGIDPIA SAIQNLKTTD KTKPSNLVNT CIRTTLDRAA CLPPGDHNAL YVNSFPLLDP SDAPFPSLDS PGKAIRGPQQ PIWKPFPNQD SDSVVLSGTD SELHIPRVCE FCQAVFPPSI TSRGDFLRHL NSHFNGET.

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.

Description:

Cytochrome B5 Reductase 2 Human Recombinant

CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.

Product # :

ENZ-799

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Description

CYB5R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a.) and having a molecular mass of 33.8kDa. CYB5R2 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

CYB5R2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cytochrome b5 reductase 2 (CYB5R2) is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. CYB5R2 is responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).
Synonyms
CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.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 MGSMNSRRRE PITLQDPEAK YPLPLIEKEK ISHNTRRFRF GLPSPDHVLG LPVGNYVQLL AKIDNELVVR AYTPVSSDDD RGFVDLIIKI YFKNVHPQYP EGGKMTQYLE NMKIGETIFF RGPRGRLFYH GPGNLGIRPD QTSEPKKTLA DHLGMIAGGT GITPMLQLIR HITKDPSDRT RMSLIFANQT EEDILVRKEL EEIARTHPDQ FNLWYTLDRP PIGWKYSSGF VTADMIKEHL PPPAKSTLIL VCGPPPLIQT AAHPNLEKLG YTQDMIFTY.

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.

Description:

Mitochondrial Ribosome Recycling Factor Human Recombinant

MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.

Product # :

PRO-1299

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Shipped with Ice Packs

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Description

MRRF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (56-262 a.a.) and having a molecular mass of 25.1kDa.MRRF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MRRF protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 30% glycerol and 2mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Mitochondrial Ribosome Recycling Factor (MRRF) is a member of the RRF family. MRRF attaches to the large ribosomal subunit in the cleft which has a peptidyl transferase center. MRRF controls the release of ribosome from messenger RNA at the termination of protein biosynthesis. Also, it may intensify the efficacy of translation by recycling ribosome from one round of translation to another.
Synonyms
MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.
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 MATKKAKAKG KGQSQTRVNI NAALVEDIIN LEEVNEEMKS VIEALKDNFN KTLNIRTSPG SLDKIAVVTA DGKLALNQIS QISMKSPQLI LVNMASFPEC TAAAIKAIRE SGMNLNPEVE GTLIRVPIPQ VTREHREMLV KLAKQNTNKA KDSLRKVRTN SMNKLKKSKD TVSEDTIRLI EKQISQMADD TVAELDRHLA VKTKELLG.

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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